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  • Chemistry  (243)
  • Cloning, Molecular  (233)
  • Cell & Developmental Biology
  • Inorganic Chemistry
  • Polymer and Materials Science
  • American Association for the Advancement of Science (AAAS)  (480)
  • 2015-2019  (235)
  • 1990-1994  (245)
  • 1965-1969
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  • 1
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2016-07-08
    Description: Separation and purification are critical industrial processes for separating components of chemical mixtures, and these processes account for about half of industrial energy usage (1). Gas mixtures of compounds with very similar physical properties are particularly difficult to separate. On pages 137 and 141 of this issue, Cadiau et al. (2) and Cui et al. (3), respectively, show that microporous materials can be designed to have high adsorption capacity and selectivity for particular hydrocarbons, enabling energy-efficient separation. Author: Jerry Y. S. Lin
    Keywords: Chemistry
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  • 2
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2016-05-27
    Description: Biomass-degrading microorganisms use lytic polysaccharide monooxygenase (LPMO) enzymes to help digest cellulose, chitin, and starch. By cleaving otherwise inaccessible crystalline cellulose chains, these enzymes provide access to hydrolytic enzymes. LPMOs are of interest to biotechnology because efficient depolymerization of cellulose is a major bottleneck for the production of biologically based chemicals and fuels. On page 1098 of this issue, Kracher et al. (1) compare LPMO-reducing substrates in fungi from different taxonomic groups and lifestyles, based on both biochemical and genomic evidence. The results provide insights into reductive activation of LPMO that are important for developing more efficient industrial enzymes for lignocellulose biorefineries. Author: Angel T. Martínez
    Keywords: Chemistry
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  • 3
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2016-03-25
    Description: Author: Marc S. Lavine
    Keywords: Chemistry
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  • 4
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2018-02-16
    Keywords: Chemistry
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  • 5
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2018-02-16
    Description: The comment and response concerning the report of oxidation of methane to methanol by water (Reports, 5 May 2017, p. 523) do not fully capture the implications of thermodynamic limitations. A nonisothermal process in which each cycle requires a large temperature swing and permits only substoichiometric methane conversion surely could not be carried out on any practical scale.
    Keywords: Chemistry
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  • 6
    Publication Date: 2018-02-16
    Description: Labinger argues that stepwise reaction of methane with water to produce methanol and hydrogen will never be commercially feasible because of its substoichiometric basis with respect to the active site and the requirement of a large temperature swing. This comment is not touching any new ground, beyond describing the thermodynamic feasibility, thermal cycling, and the role of water as discussed previously. Most important, it does not have a solid numerical basis.
    Keywords: Chemistry
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  • 7
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2018-07-27
    Keywords: Chemistry
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  • 8
    Publication Date: 2018-07-27
    Description: Vinyl carbocations have been the subject of extensive experimental and theoretical studies over the past five decades. Despite this long history in chemistry, the utility of vinyl cations in chemical synthesis has been limited, with most reactivity studies focusing on solvolysis reactions or intramolecular processes. Here we report synthetic and mechanistic studies of vinyl cations generated through silylium–weakly coordinating anion catalysis. We find that these reactive intermediates undergo mild intermolecular carbon-carbon bond–forming reactions, including carbon-hydrogen (C–H) insertion into unactivated sp 3 C–H bonds and reductive Friedel-Crafts reactions with arenes. Moreover, we conducted computational studies of these alkane C–H functionalization reactions and discovered that they proceed through nonclassical, ambimodal transition structures. This reaction manifold provides a framework for the catalytic functionalization of hydrocarbons using simple ketone derivatives.
    Keywords: Chemistry
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  • 9
    Publication Date: 2018-06-22
    Description: It is commonly assumed that recognition and discrimination of chirality, both in nature and in artificial systems, depend solely on spatial effects. However, recent studies have suggested that charge redistribution in chiral molecules manifests an enantiospecific preference in electron spin orientation. We therefore reasoned that the induced spin polarization may affect enantiorecognition through exchange interactions. Here we show experimentally that the interaction of chiral molecules with a perpendicularly magnetized substrate is enantiospecific. Thus, one enantiomer adsorbs preferentially when the magnetic dipole is pointing up, whereas the other adsorbs faster for the opposite alignment of the magnetization. The interaction is not controlled by the magnetic field per se, but rather by the electron spin orientations, and opens prospects for a distinct approach to enantiomeric separations.
    Keywords: Chemistry
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  • 10
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2018-06-29
    Keywords: Chemistry
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  • 11
    Publication Date: 2018-12-14
    Description: Theory has established the importance of geometric phase (GP) effects in the adiabatic dynamics of molecular systems with a conical intersection connecting the ground- and excited-state potential energy surfaces, but direct observation of their manifestation in chemical reactions remains a major challenge. Here, we report a high-resolution crossed molecular beams study of the H + HD -〉 H 2 + D reaction at a collision energy slightly above the conical intersection. Velocity map ion imaging revealed fast angular oscillations in product quantum state–resolved differential cross sections in the forward scattering direction for H 2 products at specific rovibrational levels. The experimental results agree with adiabatic quantum dynamical calculations only when the GP effect is included.
    Keywords: Chemistry
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  • 12
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2018-08-17
    Keywords: Chemistry
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  • 13
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2018-08-17
    Keywords: Chemistry
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  • 14
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2018-08-17
    Description: The chemistry of the carbonyl group is essential to modern organic synthesis. The preparation of substituted, enantioenriched 1,3- or 1,5-dicarbonyls is well developed, as their disconnection naturally follows from the intrinsic polarity of the carbonyl group. By contrast, a general enantioselective access to quaternary stereocenters in acyclic 1,4-dicarbonyl systems remains an unresolved problem, despite the tremendous importance of 2,3-substituted 1,4-dicarbonyl motifs in natural products and drug scaffolds. Here we present a broad enantioselective and stereodivergent strategy to access acyclic, polysubstituted 1,4-dicarbonyls via acid-catalyzed [3,3]-sulfonium rearrangement starting from vinyl sulfoxides and ynamides. The stereochemistry at sulfur governs the absolute sense of chiral induction, whereas the double bond geometry dictates the relative configuration of the final products.
    Keywords: Chemistry
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  • 15
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2018-08-17
    Keywords: Chemistry
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  • 16
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2018-08-17
    Description: With the recent soaring production of natural gas, the use of methane and other light hydrocarbon feedstocks as starting materials in synthetic transformations is becoming increasingly economically attractive, although it remains chemically challenging. We report the development of photocatalytic C–H amination, alkylation, and arylation of methane, ethane, and higher alkanes under visible light irradiation at ambient temperature. High catalytic efficiency (turnover numbers up to 2900 for methane and 9700 for ethane) and selectivity were achieved using abundant, inexpensive cerium salts as photocatalysts. Ligand-to-metal charge transfer excitation generated alkoxy radicals from simple alcohols that in turn acted as hydrogen atom transfer catalysts. The mixed-phase gas/liquid reaction was adapted to continuous flow, enabling the efficient use of gaseous feedstocks in scalable photocatalytic transformations.
    Keywords: Chemistry
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  • 17
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2018-08-24
    Keywords: Chemistry
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  • 18
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2018-08-24
    Keywords: Chemistry
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  • 19
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2018-08-31
    Keywords: Chemistry
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  • 20
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2018-08-31
    Description: Intrigued by the potential of nanoscale machines, scientists have long attempted to control molecular motion. We monitored the individual 0.7-nanometer steps of a single molecular hopper as it moved in an electric field along a track in a nanopore controlled by a chemical ratchet. The hopper demonstrated characteristics desired in a moving molecule: defined start and end points, processivity, no chemical fuel requirement, directional motion, and external control. The hopper was readily functionalized to carry cargos. For example, a DNA molecule could be ratcheted along the track in either direction, a prerequisite for nanopore sequencing.
    Keywords: Chemistry
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  • 21
    Publication Date: 2018-09-21
    Description: Phosphorothioate nucleotides have emerged as powerful pharmacological substitutes of their native phosphodiester analogs with important translational applications in antisense oligonucleotide (ASO) therapeutics and cyclic dinucleotide (CDN) synthesis. Stereocontrolled installation of this chiral motif has long been hampered by the systemic use of phosphorus(III) [P(III)]–based reagent systems as the sole practical means of oligonucleotide assembly. A fundamentally different approach is described herein: the invention of a P(V)-based reagent platform for programmable, traceless, diastereoselective phosphorus-sulfur incorporation. The power of this reagent system is demonstrated through the robust and stereocontrolled synthesis of various nucleotidic architectures, including ASOs and CDNs, via an efficient, inexpensive, and operationally simple protocol.
    Keywords: Chemistry
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  • 22
    Publication Date: 2018-09-21
    Description: Here we report an anomalous porous molecular crystal built of C–H···N-bonded double-layered roof-floor components and wall components of a segregatively interdigitated architecture. This complicated porous structure consists of only one type of fully aromatic multijoint molecule carrying three identical dipyridylphenyl wedges. Despite its high symmetry, this molecule accomplishes difficult tasks by using two of its three wedges for roof-floor formation and using its other wedge for wall formation. Although a C–H···N bond is extremely labile, the porous crystal maintains its porosity until thermal breakdown of the C–H···N bonds at 202°C occurs, affording a nonporous polymorph. Though this nonporous crystal survives even at 325°C, it can retrieve the parent porosity under acetonitrile vapor. These findings show how one can translate simplicity into ultrahigh complexity.
    Keywords: Chemistry
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  • 23
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2018-09-28
    Keywords: Chemistry
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  • 24
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2018-09-28
    Keywords: Chemistry
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  • 25
    Publication Date: 2018-09-28
    Description: Some of the simplest and most powerful carbon-carbon bond forming strategies take advantage of readily accessible ubiquitous motifs: carbonyls and olefins. Here we report a fundamentally distinct mode of reactivity between carbonyls and olefins that differs from established acid-catalyzed carbonyl-ene, Prins, and carbonyl-olefin metathesis reaction paths. A range of epsilon, zeta-unsaturated ketones undergo Brønsted acid–catalyzed intramolecular cyclization to provide tetrahydrofluorene products via the formation of two new carbon-carbon bonds. Theoretical calculations and accompanying mechanistic studies suggest that this carbocyclization reaction proceeds through the intermediacy of a transient oxetane formed by oxygen atom transfer. The complex polycyclic frameworks in this product class appear as common substructures in organic materials, bioactive natural products, and recently developed pharmaceuticals.
    Keywords: Chemistry
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  • 26
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2018-09-28
    Description: Alkene aminoarylation with a single, bifunctional reagent is a concise synthetic strategy. We report a catalytic protocol for the addition of arylsulfonylacetamides across electron-rich alkenes with complete anti-Markovnikov regioselectivity and excellent diastereoselectivity to provide 2,2-diarylethylamines. In this process, single-electron alkene oxidation enables carbon-nitrogen bond formation to provide a key benzylic radical poised for a Smiles-Truce 1,5-aryl shift. This reaction is redox-neutral, exhibits broad functional group compatibility, and occurs at room temperature with loss of sulfur dioxide. As this process is driven by visible light, uses readily available starting materials, and demonstrates convergent synthesis, it is well suited for use in a variety of synthetic endeavors.
    Keywords: Chemistry
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  • 27
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2018-10-05
    Keywords: Chemistry
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  • 28
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2018-10-05
    Keywords: Chemistry
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  • 29
    Publication Date: 2018-10-05
    Description: Photocatalysis based on optically active, "plasmonic" metal nanoparticles has emerged as a promising approach to facilitate light-driven chemical conversions under far milder conditions than thermal catalysis. However, an understanding of the relation between thermal and electronic excitations has been lacking. We report the substantial light-induced reduction of the thermal activation barrier for ammonia decomposition on a plasmonic photocatalyst. We introduce the concept of a light-dependent activation barrier to account for the effect of light illumination on electronic and thermal excitations in a single unified picture. This framework provides insight into the specific role of hot carriers in plasmon-mediated photochemistry, which is critically important for designing energy-efficient plasmonic photocatalysts.
    Keywords: Chemistry
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  • 30
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2018-10-12
    Keywords: Chemistry
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  • 31
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2018-10-12
    Keywords: Chemistry
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  • 32
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2018-10-12
    Description: Single-electron reduction of a carbonyl to a ketyl enables access to a polarity-reversed platform of reactivity for this cornerstone functional group. However, the synthetic utility of the ketyl radical is hindered by the strong reductants necessary for its generation, which also limit its reactivity to net reductive mechanisms. We report a strategy for net redox-neutral generation and reaction of ketyl radicals. The in situ conversion of aldehydes to α-acetoxy iodides lowers their reduction potential by more than 1 volt, allowing for milder access to the corresponding ketyl radicals and an oxidative termination event. Upon subjecting these iodides to a dimanganese decacarbonyl precatalyst and visible light irradiation, an atom transfer radical addition (ATRA) mechanism affords a broad scope of vinyl iodide products with high Z -selectivity.
    Keywords: Chemistry
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  • 33
    Publication Date: 2018-10-12
    Description: Reactions that form a product with the same reactive functionality as that of one of the starting compounds frequently end in oligomerization. As a salient example, selective aldol coupling of the smallest, though arguably most useful, enolizable aldehyde, acetaldehyde, with just one partner substrate has proven to be extremely challenging. Here, we report a highly enantioselective Mukaiyama aldol reaction with the simple triethylsilyl (TES) and tert -butyldimethylsilyl (TBS) enolates of acetaldehyde and various aliphatic and aromatic acceptor aldehydes. The reaction is catalyzed by recently developed, strongly acidic imidodiphosphorimidates (IDPi), which, like enzymes, display a confined active site but, like small-molecule catalysts, have a broad substrate scope. The process is scalable, fast, efficient (0.5 to 1.5 mole % catalyst loading), and greatly simplifies access to highly valuable silylated acetaldehyde aldols.
    Keywords: Chemistry
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  • 34
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2018-12-21
    Keywords: Chemistry
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  • 35
    Publication Date: 2018-12-21
    Description: Single-molecule magnets (SMMs) containing only one metal center may represent the lower size limit for molecule-based magnetic information storage materials. Their current drawback is that all SMMs require liquid-helium cooling to show magnetic memory effects. We now report a chemical strategy to access the dysprosium metallocene cation [(Cp i Pr5 )Dy(Cp*)] + (Cp i Pr5 , penta-iso-propylcyclopentadienyl; Cp *, pentamethylcyclopentadienyl), which displays magnetic hysteresis above liquid-nitrogen temperatures. An effective energy barrier to reversal of the magnetization of U eff = 1541 wave number is also measured. The magnetic blocking temperature of T B = 80 kelvin for this cation overcomes an essential barrier toward the development of nanomagnet devices that function at practical temperatures.
    Keywords: Chemistry
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  • 36
    Publication Date: 1990-06-01
    Description: Better understanding of the pathogenesis of acquired immunodeficiency syndrome (AIDS) would be greatly facilitated by a relevant animal model that uses molecularly cloned virus of defined sequence to induce the disease. Such a system would also be of great value for AIDS vaccine research. An infectious molecular clone of simian immunodeficiency virus (SIV) was identified that induces AIDS in common rhesus monkeys in a time frame suitable for laboratory investigation. These results provide another strong link in the chain of evidence for the viral etiology of AIDS. More importantly, they define a system for molecular dissection of the determinants of AIDS pathogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kestler, H -- Kodama, T -- Ringler, D -- Marthas, M -- Pedersen, N -- Lackner, A -- Regier, D -- Sehgal, P -- Daniel, M -- King, N -- AI25328/AI/NIAID NIH HHS/ -- RR00168/RR/NCRR NIH HHS/ -- RR00169/RR/NCRR NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1990 Jun 1;248(4959):1109-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉New England Regional Primate Research Center, Harvard Medical School, Southborough, MA 01772.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2160735" target="_blank"〉PubMed〈/a〉
    Keywords: *Acquired Immunodeficiency Syndrome ; Animals ; Antibodies, Viral/biosynthesis ; Cloning, Molecular ; *Disease Models, Animal ; Leukocytes, Mononuclear/microbiology ; Macaca mulatta ; Macrophages/microbiology ; Opportunistic Infections/etiology ; *Retroviridae Infections/complications/immunology ; *Simian Immunodeficiency Virus/genetics/immunology/isolation & ; purification/pathogenicity ; Transfection ; Virus Replication
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  • 37
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-04-27
    Description: Light-dependent expression of rbcS, the gene encoding the small subunit of ribulose-1,5-bisphosphate carboxylase, which is the key enzyme involved in carbon fixation in higher plants, is regulated at the transcriptional level. Sequence analysis of the gene has uncovered a conserved GT motif in the -150 to -100 region of many rbcS promoters. This motif serves as the binding site of a nuclear factor, designated GT-1. Analysis of site-specific mutants of pea rbcS-3A promoter demonstrated that GT-1 binding in vitro is correlated with light-responsive expression of the rbcS promoter in transgenic plants. However, it is not known whether factors other than GT-1 might also be required for activation of transcription by light. A synthetic tetramer of box II (TGTGTGGTTAATATG), the GT-1 binding site located between -152 to -138 of the rbcS-3A promoter, inserted upstream of a truncated cauliflower mosaic virus 35S promoter is sufficient to confer expression in leaves of transgenic tobacco. This expression occurs principally in chloroplast-containing cells, is induced by light, and is correlated with the ability of box II to bind GT-1 in vitro. The data show that the binding site for GT-1 is likely to be a part of the molecular light switch for rbcS activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lam, E -- Chua, N H -- New York, N.Y. -- Science. 1990 Apr 27;248(4954):471-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Plant Molecular Biology, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2330508" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Chloramphenicol O-Acetyltransferase/genetics ; Cloning, Molecular ; DNA-Binding Proteins/*metabolism ; Gene Expression Regulation/*physiology ; Genetic Vectors ; *Light ; Molecular Sequence Data ; Mutation ; Nuclear Proteins/*metabolism ; Plant Proteins/*metabolism ; *Plants, Toxic ; Promoter Regions, Genetic/genetics ; Ribulose-Bisphosphate Carboxylase/*genetics ; Tobacco/enzymology/*genetics ; Transcription, Genetic/radiation effects ; Transformation, Genetic
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  • 38
    Publication Date: 1990-06-29
    Description: The human immunodeficiency virus (HIV) tat protein (Tat) is a positive regulator of virus gene expression and replication. Biotinylated Tat was used as a probe to screen a lambda gt11 fusion protein library, and a complementary DNA encoding a protein that interacts with Tat was cloned. Expression of this protein, designated TBP-1 (for Tat binding protein-1), was observed in a variety of cell lines, with expression being highest in human cells. TBP-1 was localized predominantly in the nucleus, which is consistent with the nuclear localization of Tat. In cotransfection experiments, expression of TBP-1 was able to specifically suppress Tat-mediated transactivation. The strategy described may be useful for direct identification and cloning of genes encoding proteins that associate with other proteins to modulate their activity in a positive or negative fashion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nelbock, P -- Dillon, P J -- Perkins, A -- Rosen, C A -- New York, N.Y. -- Science. 1990 Jun 29;248(4963):1650-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Oncology and Virology, Roche Institute of Molecular Biology, Hoffmann-La Roche Inc., Nutley, NJ 07110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2194290" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Cloning, Molecular ; DNA, Neoplasm/genetics ; DNA-Binding Proteins/*genetics/metabolism ; Escherichia coli/genetics ; Gene Expression ; Gene Library ; Gene Products, tat/*metabolism ; HIV/genetics ; Humans ; Molecular Sequence Data ; Plasmids ; Polymerase Chain Reaction ; *Proteasome Endopeptidase Complex ; Recombinant Fusion Proteins/metabolism ; Trans-Activators/*metabolism ; Transcriptional Activation ; Transfection ; tat Gene Products, Human Immunodeficiency Virus
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  • 39
    Publication Date: 1990-07-13
    Description: The heterotrimeric guanine nucleotide-binding regulatory proteins act at the inner surface of the plasma membrane to relay information from cell surface receptors to effectors inside the cell. These G proteins are not integral membrane proteins, yet are membrane associated. The processing and function of the gamma subunit of the yeast G protein involved in mating-pheromone signal transduction was found to be affected by the same mutations that block ras processing. The nature of these mutations implied that the gamma subunit was polyisoprenylated and that this modification was necessary for membrane association and biological activity. A microbial screen was developed for pharmacological agents that inhibit polyisoprenylation and that have potential application in cancer therapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Finegold, A A -- Schafer, W R -- Rine, J -- Whiteway, M -- Tamanoi, F -- CA 41996/CA/NCI NIH HHS/ -- GM 07183/GM/NIGMS NIH HHS/ -- GM 35827/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Jul 13;249(4965):165-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, University of Chicago, IL 60637.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1695391" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cell Membrane/metabolism ; Cloning, Molecular ; Epitopes/genetics ; GTP-Binding Proteins/genetics/*metabolism ; Hemagglutinins, Viral/immunology ; Lovastatin/pharmacology ; Mevalonic Acid/pharmacology ; Molecular Sequence Data ; Mutation ; Oncogene Protein p21(ras)/genetics/*metabolism ; Orthomyxoviridae/immunology ; Protein Processing, Post-Translational ; Saccharomyces cerevisiae/*genetics/metabolism ; Signal Transduction ; Suppression, Genetic
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  • 40
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-02-09
    Description: Transcription of a typical eukaryotic gene by RNA polymerase II is activated by proteins bound to sites found near the beginning of the gene as well as to sites, called enhancers, located a great distance from the gene. According to one view, the primary difference between an activator that can work at a large distance and one that cannot is that the former bears a particularly strong activating region; the stronger the activating region, the more readily the activator interacts with its target bound near the transcriptional start site, with the intervening DNA looping out to accommodate the reaction. One alternative view is that the effect of proteins bound to enhancers might require some special aspect of cellular or chromosome structure. Consistent with the first view, an activator bearing an unusually potent activating region can stimulate transcription of a mammalian gene in a HeLa nuclear extract when bound as far as 1.3 kilobase pairs upstream or 320 base pairs downstream of the transcriptional start site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carey, M -- Leatherwood, J -- Ptashne, M -- New York, N.Y. -- Science. 1990 Feb 9;247(4943):710-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2405489" target="_blank"〉PubMed〈/a〉
    Keywords: Activating Transcription Factors ; Binding Sites ; Blood Proteins/pharmacology ; Cloning, Molecular ; DNA/metabolism ; DNA-Binding Proteins ; Fungal Proteins/metabolism/*pharmacology ; HeLa Cells ; Phosphoproteins/pharmacology ; Promoter Regions, Genetic ; RNA Polymerase II/metabolism ; Recombinant Fusion Proteins/pharmacology ; *Saccharomyces cerevisiae Proteins ; Templates, Genetic ; Trans-Activators/pharmacology ; Transcription Factors/pharmacology ; Transcription, Genetic/*drug effects
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  • 41
    Publication Date: 1990-07-27
    Description: The major autophosphorylation sites of the rat beta II isozyme of protein kinase C were identified. The modified threonine and serine residues were found in the amino-terminal peptide, the carboxyl-terminal tail, and the hinge region between the regulatory lipid-binding domain and the catalytic kinase domain. Because this autophosphorylation follows an intrapeptide mechanism, extraordinary flexibility of the protein is necessary to phosphorylate the three regions. Comparison of the sequences surrounding the modified residues showed no obvious recognition motif nor any similarity to substrate phosphorylation sites, suggesting that proximity to the active site may be the primary criterion for their phosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flint, A J -- Paladini, R D -- Koshland, D E Jr -- DK09765/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1990 Jul 27;249(4967):408-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2377895" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Brain/enzymology ; Cloning, Molecular ; Isoenzymes/genetics/*metabolism ; Molecular Sequence Data ; Peptide Fragments/isolation & purification/metabolism ; Phosphorylation ; Protein Conformation ; Protein Kinase C/genetics/*metabolism ; Rats ; Recombinant Proteins/metabolism ; Signal Transduction ; Trypsin
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  • 42
    Publication Date: 1990-05-11
    Description: Chronic granulomatous diseases (CGDs) are characterized by recurrent infections resulting from impaired superoxide production by a phagocytic cell, nicotinamide adenine dinucleotide phosphate (reduced) (NADPH) oxidase. Complementary DNAs were cloned that encode the 67-kilodalton (kD) cytosolic oxidase factor (p67), which is deficient in 5% of CGD patients. Recombinant p67 (r-p67) partially restored NADPH oxidase activity to p67-deficient neutrophil cytosol from these patients. The p67 cDNA encodes a 526-amino acid protein with acidic middle and carboxyl-terminal domains that are similar to a sequence motif found in the noncatalytic domain of src-related tyrosine kinases. This motif was recently noted in phospholipase C-gamma, nonerythroid alpha-spectrin (fodrin), p21ras-guanosine triphophatase-activating protein (GAP), myosin-1 isoforms, yeast proteins cdc-25 and fus-1, and the 47-kD phagocyte oxidase factor (p47), which suggests the possibility of common regulatory features.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leto, T L -- Lomax, K J -- Volpp, B D -- Nunoi, H -- Sechler, J M -- Nauseef, W M -- Clark, R A -- Gallin, J I -- Malech, H L -- I01 BX000513/BX/BLRD VA/ -- New York, N.Y. -- Science. 1990 May 11;248(4956):727-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Clinical Investigation, National Institute of Allergy and Infectious Diseases, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1692159" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; Granulomatous Disease, Chronic/blood/enzymology/genetics ; Humans ; Molecular Sequence Data ; NADH, NADPH Oxidoreductases/blood/*genetics ; NADPH Oxidase ; Neutrophils/*enzymology ; Protein-Tyrosine Kinases/genetics ; Proto-Oncogene Proteins/*genetics ; Proto-Oncogene Proteins pp60(c-src) ; Sequence Homology, Nucleic Acid
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  • 43
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-12-21
    Description: Transcription of the mouse alpha-fetoprotein gene is activated in the developing fetal liver and gut and repressed in both tissues shortly after birth. With germline transformation in mice, a cis-acting element was identified upstream of the transcription initiation site of the alpha-fetoprotein gene that was responsible for repression of the gene in adult liver. This negative element acts as a repressor in a position-dependent manner.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vacher, J -- Tilghman, S M -- CA44976/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1990 Dec 21;250(4988):1732-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Biology, Princeton University, NJ 08544.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1702902" target="_blank"〉PubMed〈/a〉
    Keywords: Aging ; Animals ; Animals, Newborn ; Chromosome Deletion ; Cloning, Molecular ; DNA-Binding Proteins/metabolism ; Enhancer Elements, Genetic ; Fetus ; *Gene Expression Regulation ; Hepatocyte Nuclear Factor 1 ; Hepatocyte Nuclear Factor 1-alpha ; Hepatocyte Nuclear Factor 1-beta ; Liver/growth & development/*metabolism ; Mice ; *Nuclear Proteins ; Transcription Factors/metabolism ; Transcription, Genetic ; alpha-Fetoproteins/*genetics
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  • 44
    Publication Date: 1990-01-05
    Description: Cosmid clones containing human DNA inserts have been mapped on chromosome 11 by fluorescence in situ hybridization under conditions that suppress signal from repetitive DNA sequences. Thirteen known genes, one chromosome 11-specific DNA repeat, and 36 random clones were analyzed. High-resolution mapping was facilitated by using digital imaging microscopy and by analyzing extended (prometaphase) chromosomes. The map coordinates established by in situ hybridization showed a one to one correspondence with those determined by Southern (DNA) blot analysis of hybrid cell lines containing fragments of chromosome 11. Furthermore, by hybridizing three or more cosmids simultaneously, gene order on the chromosome could be established unequivocally. These results demonstrate the feasibility of rapidly producing high-resolution maps of human chromosomes by in situ hybridization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lichter, P -- Tang, C J -- Call, K -- Hermanson, G -- Evans, G A -- Housman, D -- Ward, D C -- GM-27882/GM/NIGMS NIH HHS/ -- GM-33868/GM/NIGMS NIH HHS/ -- HD-18012/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1990 Jan 5;247(4938):64-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Human Genetics, Yale University School of Medicine, New Haven, CT 06510.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2294592" target="_blank"〉PubMed〈/a〉
    Keywords: Blotting, Southern ; Cell Line ; *Chromosome Mapping ; *Chromosomes, Human, Pair 11 ; Cloning, Molecular ; Cosmids/*genetics ; DNA/*genetics ; DNA Probes ; Fluorescent Dyes ; Humans ; Hybrid Cells ; Microscopy, Fluorescence ; *Nucleic Acid Hybridization ; Repetitive Sequences, Nucleic Acid
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  • 45
    Publication Date: 1990-06-22
    Description: Homologous or agonist-specific desensitization of beta-adrenergic receptors is thought to be mediated by a specific kinase, the beta-adrenergic receptor kinase (beta ARK). However, recent data suggest that a cofactor is required for this kinase to inhibit receptor function. The complementary DNA for such a cofactor was cloned and found to encode a 418-amino acid protein homologous to the retinal protein arrestin. The protein, termed beta-arrestin, was expressed and partially purified. It inhibited the signaling function of beta ARK-phosphorylated beta-adrenergic receptors by more than 75 percent, but not that of rhodopsin. It is proposed that beta-arrestin in concert with beta ARK effects homologous desensitization of beta-adrenergic receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lohse, M J -- Benovic, J L -- Codina, J -- Caron, M G -- Lefkowitz, R J -- DK19318/DK/NIDDK NIH HHS/ -- HL16037/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1990 Jun 22;248(4962):1547-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Medicine, Biochemistry and Cell Biology, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2163110" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens/*genetics/isolation & purification/pharmacology ; Arrestin ; Blotting, Northern ; Chromatography, Ion Exchange ; Cloning, Molecular ; *Cyclic AMP-Dependent Protein Kinases ; DNA/genetics ; Eye Proteins/*genetics/isolation & purification/pharmacology ; Gene Expression Regulation ; Molecular Sequence Data ; Phosphodiesterase Inhibitors/*pharmacology ; Phosphorylation ; Protein Kinases/*pharmacology ; RNA, Messenger/analysis ; Receptors, Adrenergic, beta/*drug effects/physiology ; Transfection ; beta-Adrenergic Receptor Kinases
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  • 46
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-08-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Waldrop, M M -- New York, N.Y. -- Science. 1990 Aug 3;249(4968):472-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2382127" target="_blank"〉PubMed〈/a〉
    Keywords: Chemical Phenomena ; Chemistry ; *Information Systems ; Jurisprudence ; Societies, Scientific ; United States
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  • 47
    Publication Date: 1990-05-25
    Description: A subline of U937 cells (U937D) was obtained in which creatine kinase B (CK-B) messenger RNA was present and bound to ribosomes, but CK activity was undetectable. Transformation of U937D cells with retrovirus vectors that contain the 3' untranslated region (3' UTR) of CK-B messenger RNA exhibited CK activity with no change in abundance of CK-B mRNA. The 3' UTR formed a complex in vitro with a component of S100 extracts from wild-type cells. This binding activity was not detectable in S100 extracts from cells that expressed CK activity after transformation with the 3' UTR-containing vector. These results suggest that translation of CK-B is repressed by binding of a soluble factor or factors to the 3' UTR.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ch'ng, J L -- Shoemaker, D L -- Schimmel, P -- Holmes, E W -- GM34366/GM/NIGMS NIH HHS/ -- R01-CA 47631-02/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1990 May 25;248(4958):1003-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Duke University, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2343304" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; Cloning, Molecular ; Creatine Kinase/*genetics ; *Gene Expression Regulation ; Humans ; Hypoxanthine Phosphoribosyltransferase/genetics ; Polyribosomes/metabolism ; *Protein Biosynthesis ; RNA, Messenger/*genetics
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  • 48
    Publication Date: 1990-08-17
    Description: Primary and secondary hypertriglyceridemia is common in the general population, but the biochemical basis for this disease is largely unknown. With the use of transgenic technology, two lines of mice were created that express the human apolipoprotein CIII gene. One of these mouse lines with 100 copies of the gene was found to express large amounts of the protein and to be severely hypertriglyceridemic. The other mouse line with one to two copies of the gene expressed low amounts of the protein, but nevertheless manifested mild hypertriglyceridemia. Thus, overexpression of apolipoprotein CIII can be a primary cause of hypertriglyceridemia in vivo and may provide one possible etiology for this common disorder in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ito, Y -- Azrolan, N -- O'Connell, A -- Walsh, A -- Breslow, J L -- HL 36461/HL/NHLBI NIH HHS/ -- HL33435/HL/NHLBI NIH HHS/ -- HL33714/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1990 Aug 17;249(4970):790-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2167514" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apolipoprotein C-III ; Apolipoproteins C/blood/*genetics ; Chylomicrons/blood ; Cloning, Molecular ; DNA Restriction Enzymes/metabolism ; DNA, Recombinant/metabolism ; *Gene Expression ; Humans ; Hypertriglyceridemia/blood/*genetics ; Lipoproteins, VLDL/blood ; Mice ; Mice, Inbred C57BL ; Mice, Inbred CBA ; Mice, Transgenic ; Nucleic Acid Hybridization ; RNA, Messenger/genetics ; Triglycerides/blood
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  • 49
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-06-01
    Description: A heat shock protein gene, HSP104, was isolated from Saccharomyces cerevisiae and a deletion mutation was introduced into yeast cells. Mutant cells grew at the same rate as wild-type cells and died at the same rate when exposed directly to high temperatures. However, when given a mild pre-heat treatment, the mutant cells did not acquire tolerance to heat, as did wild-type cells. Transformation with the wild-type gene rescued the defect of mutant cells. The results demonstrate that a particular heat shock protein plays a critical role in cell survival at extreme temperatures.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sanchez, Y -- Lindquist, S L -- GM 35483/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Jun 1;248(4959):1112-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular Genetics and Cell Biology, University of Chicago, Illinois 60637.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2188365" target="_blank"〉PubMed〈/a〉
    Keywords: Cloning, Molecular ; Fungal Proteins/biosynthesis/*genetics ; Genes, Fungal ; Heat-Shock Proteins/biosynthesis/genetics/*physiology ; *Hot Temperature ; Mutation ; Restriction Mapping ; Saccharomyces cerevisiae/genetics/growth & development/*physiology
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  • 50
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-12-07
    Description: The mammalian olfactory system may transduce odorant information via a G protein-mediated adenosine 3',5'-monophosphate (cAMP) cascade. A newly discovered adenylyl cyclase, termed type III, has been cloned, and its expression was localized to olfactory neurons. The type III protein resides in the sensory neuronal cilia, which project into the nasal lumen and are accessible to airborne odorants. The enzymatic activity of the type III adenylyl cyclase appears to differ from nonsensory cyclases. The large difference seen between basal and stimulated activity for the type III enzyme could allow considerable modulation of the intracellular cAMP concentration. This property may represent one mechanism of achieving sensitivity in odorant perception.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bakalyar, H A -- Reed, R R -- 5T32CA09339/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1990 Dec 7;250(4986):1403-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Genetics, Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2255909" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/genetics/*physiology ; Amino Acid Sequence ; Animals ; Brain/enzymology/physiology ; Cell Line ; Clone Cells ; Cloning, Molecular ; Gene Library ; Glycosylation ; Isoenzymes/genetics/*physiology ; Macromolecular Substances ; Molecular Sequence Data ; Molecular Weight ; Neurons, Afferent/enzymology/physiology ; Nose/enzymology/physiology ; *Odors ; Protein Conformation ; Rats ; *Signal Transduction
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  • 51
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-03-15
    Description: The abdominal ganglion of the marine mollusk Aplysia contains a pair of identified neuronal clusters, the bag cells, which control egg laying by means of a number of unique regulatory mechanisms. Each neuron in the bag cell clusters synthesizes several peptides derived from a single prohormone and packages them into separate vesicles. These vesicles are then differentially localized in specific neuronal processes, thus segregating peptides destined for autocrine and hormonal release sites. Therefore in this system, protein trafficking through the secretory pathway organizes multiple peptide neurochemical messengers to efficiently regulate simple behaviors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jung, L J -- Scheller, R H -- New York, N.Y. -- Science. 1991 Mar 15;251(4999):1330-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, Beckman Center, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2003219" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aplysia/genetics/*physiology ; Cell Compartmentation ; Cloning, Molecular ; DNA/genetics ; Invertebrate Hormones/genetics/*metabolism ; Neuropeptides/*physiology ; Neurosecretory Systems/*physiology ; Protein Precursors/metabolism ; Protein Processing, Post-Translational ; Sexual Behavior, Animal/physiology ; Transfection
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  • 52
    Publication Date: 1991-10-25
    Description: The presence of clathrate hydrates in cometary ice has been suggested to account for anomalous gas release at large radial distances from the sun as well as the retention of volatiles in comets to elevated temperatures. However, how clathrate hydrates can form in low-pressure environments, such as in cold interstellar molecular clouds, in the outer reaches of the early solar nebula, or in cometary ices, has been poorly understood. Experiments performed with the use of a modified electron microscope demonstrate that during the warming of vapor-deposited amorphous ices in vacuo, clathrate hydrates can form by rearrangements in the solid state. Phase separations and microporous textures that are the result of these rearrangements may account for a variety of anomalous cometary phenomena.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Blake, D -- Allamandola, L -- Sandford, S -- Hudgins, D -- Freund, F -- New York, N.Y. -- Science. 1991 Oct 25;254:548-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Planetary Biology Branch, Ames Research Center, Moffett Field, CA 94035, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11538372" target="_blank"〉PubMed〈/a〉
    Keywords: Chemical Phenomena ; Chemistry ; Crystallography ; Earth (Planet) ; Hydrocarbons/chemistry ; Ice/*analysis ; *Meteoroids ; Microscopy, Electron ; *Solar System
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  • 53
    Publication Date: 1991-05-31
    Description: An in vivo selection system for isolating targets of DNA binding proteins in yeast was developed and used to identify the DNA binding site for the NGFI-B protein, a member of the steroid-thyroid hormone receptor superfamily. The feasibility of the technique was verified by selecting DNA fragments that contained binding sites for GCN4, a well-characterized yeast transcriptional activator. The DNA binding domain of NGFI-B, expressed as part of a LexA-NGFI-B-GAL4 chimeric activator, was then used to isolate a rat genomic DNA fragment that contained an NGFI-B binding site. The NGFI-B response element (NBRE) is similar to but functionally distinct from elements recognized by the estrogen and thyroid hormone receptors and the hormone receptor-like proteins COUP-TF, CF1, and H-2RIIBP. Cotransfection experiments in mammalian cells demonstrated that NGFI-B can activate transcription from the NBRE with or without its putative ligand binding domain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, T E -- Fahrner, T J -- Johnston, M -- Milbrandt, J -- NS01018/NS/NINDS NIH HHS/ -- P01 CA49712/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 May 31;252(5010):1296-300.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925541" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Proteins/metabolism ; Base Sequence ; Binding Sites ; Cloning, Molecular ; DNA, Fungal/*metabolism ; DNA-Binding Proteins/genetics/*metabolism/pharmacology ; Fungal Proteins/metabolism ; Molecular Sequence Data ; Nuclear Receptor Subfamily 4, Group A, Member 1 ; Plasmids ; *Protein Kinases ; Rats ; Receptors, Cytoplasmic and Nuclear ; Receptors, Steroid ; Repressor Proteins ; Saccharomyces cerevisiae/*genetics ; *Saccharomyces cerevisiae Proteins ; *Serine Endopeptidases ; Transcription Factors/genetics/*metabolism/pharmacology ; Transcription, Genetic ; Transfection
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  • 54
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-10-25
    Description: The action of dopamine and other monoamine neurotransmitters at synapses is terminated predominantly by high-affinity reuptake into presynaptic terminals by specific sodium-dependent neurotransmitter transport proteins. A complementary DNA encoding a rat dopamine transporter has been isolated that exhibits high sequence similarity with the previously cloned norepinephrine and gamma-aminobutyric acid transporters. Transient expression of the complementary DNA in HeLa cells confirms the cocaine sensitivity of this transporter.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kilty, J E -- Lorang, D -- Amara, S G -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):578-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Yale University, New Haven, CT 06510.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948035" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Carrier Proteins/drug effects/*genetics/metabolism ; Cloning, Molecular ; Cocaine/*pharmacology ; Dopamine/*metabolism ; Dopamine Plasma Membrane Transport Proteins ; Gene Expression ; HeLa Cells ; Humans ; Kinetics ; *Membrane Glycoproteins ; *Membrane Transport Proteins ; Molecular Sequence Data ; *Nerve Tissue Proteins ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction/methods ; Rats ; Sequence Homology, Nucleic Acid ; Transfection
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  • 55
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-02-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J -- New York, N.Y. -- Science. 1991 Feb 22;251(4996):876-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1900373" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*genetics ; Amyloid beta-Peptides/*genetics ; Amyloid beta-Protein Precursor ; Chromosomes, Human, Pair 21 ; Cloning, Molecular ; Humans ; *Mutation ; Protein Precursors/*genetics
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  • 56
    Publication Date: 1991-02-22
    Description: The structure of the ion conduction pathway or pore of voltage-gated ion channels is unknown, although the linker between the membrane spanning segments S5 and S6 has been suggested to form part of the pore in potassium channels. To test whether this region controls potassium channel conduction, a 21-amino acid segment of the S5-S6 linker was transplanted from the voltage-activated potassium channel NGK2 to another potassium channel DRK1, which has very different pore properties. In the resulting chimeric channel, the single channel conductance and blockade by external and internal tetraethylammonium (TEA) ion were characteristic of the donor NGK2 channel. Thus, this 21-amino acid segment controls the essential biophysical properties of the pore and may form the conduction pathway of these potassium channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hartmann, H A -- Kirsch, G E -- Drewe, J A -- Taglialatela, M -- Joho, R H -- Brown, A M -- NS08805/NS/NINDS NIH HHS/ -- NS23877/NS/NINDS NIH HHS/ -- NS28407/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Feb 22;251(4996):942-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Physiology and Biophysics, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2000495" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Brain/physiology ; Chimera ; Cloning, Molecular ; Female ; Ion Channel Gating ; Membrane Potentials ; Molecular Sequence Data ; Oligonucleotide Probes ; Oocytes/physiology ; Polymerase Chain Reaction ; Potassium Channels/drug effects/genetics/*physiology ; Rats ; Restriction Mapping ; Sequence Homology, Nucleic Acid ; Tetraethylammonium ; Tetraethylammonium Compounds/pharmacology ; Xenopus
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  • 57
    Publication Date: 1991-07-05
    Description: Molecular cloning of the t(10;14)(q24;q11) recurrent breakpoint of T cell acute lymphoblastic leukemia has demonstrated a transcript for the candidate gene TCL3. Characterization of this gene from chromosome segment 10q24 revealed it to be a new homeobox, HOX11. The HOX11 homeodomain is most similar to that of the murine gene Hlx and possesses a markedly glycine-rich variable region and an acidic carboxyl terminus. HOX11, while expressed in liver, was not detected in normal thymus or T cells. This lineage-restricted homeobox gene is deregulated upon translocation into the T cell receptor locus where it may act as an oncogene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hatano, M -- Roberts, C W -- Minden, M -- Crist, W M -- Korsmeyer, S J -- 1 PO1 CA49712/CA/NCI NIH HHS/ -- CA 21765/CA/NCI NIH HHS/ -- CA 30969/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 5;253(5015):79-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1676542" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Northern ; Chromosomes, Human, Pair 10 ; Chromosomes, Human, Pair 14 ; Cloning, Molecular ; *Gene Expression Regulation, Neoplastic ; *Genes, Homeobox ; Humans ; Leukemia-Lymphoma, Adult T-Cell/*genetics ; Mice ; Molecular Sequence Data ; Receptors, Antigen, T-Cell/genetics ; Restriction Mapping ; Sequence Homology, Nucleic Acid ; *Translocation, Genetic
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  • 58
    Publication Date: 1991-04-05
    Description: The natriuretic peptides are hormones that can stimulate natriuretic, diuretic, and vasorelaxant activity in vivo, presumably through the activation of two known cell surface receptor guanylyl cyclases (ANPR-A and ANPR-B). Although atrial natriuretic peptide (ANP) and, to a lesser extent, brain natriuretic peptide (BNP) are efficient activators of the ANPR-A guanylyl cyclase, neither hormone can significantly stimulate ANPR-B. A member of this hormone family, C-type natriuretic peptide (CNP), potently and selectively activated the human ANPR-B guanylyl cyclase. CNP does not increase guanosine 3',5'-monophosphate accumulation in cells expressing human ANPR-A. The affinity of CNP for ANPR-B is 50- or 500-fold higher than ANP or BNP, respectively. This ligand-receptor pair may be involved in the regulation of fluid homeostasis by the central nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koller, K J -- Lowe, D G -- Bennett, G L -- Minamino, N -- Kangawa, K -- Matsuo, H -- Goeddel, D V -- New York, N.Y. -- Science. 1991 Apr 5;252(5002):120-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Genentech, Inc., South San Francisco 94080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1672777" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Atrial Natriuretic Factor/*physiology ; Cells, Cultured ; Cercopithecus aethiops ; Cloning, Molecular ; Dose-Response Relationship, Drug ; Guanylate Cyclase/metabolism ; Humans ; Natriuretic Peptide, Brain ; Natriuretic Peptide, C-Type ; Nerve Tissue Proteins/*pharmacology ; Receptors, Atrial Natriuretic Factor ; Receptors, Cell Surface/*physiology ; Recombinant Proteins ; Signal Transduction
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  • 59
    Publication Date: 1991-10-18
    Description: Dioxin (2,3,7,8-tetrachlorodibenzo-p-dioxin, TCDD), a widespread environmental contaminant, may elicit its effects by altering gene expression in susceptible cells. Five TCDD-responsive complementary DNA clones were isolated from a human keratinocyte cell line. One of these clones encodes plasminogen activator inhibitor-2, a factor that influences growth and differentiation by regulating proteolysis of the extracellular matrix. Another encodes the cytokine interleukin-1 beta. Thus, TCDD alters the expression of growth regulatory genes and has effects similar to those of other tumor-promoting agents that affect both inflammation and differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sutter, T R -- Guzman, K -- Dold, K M -- Greenlee, W F -- New York, N.Y. -- Science. 1991 Oct 18;254(5030):415-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Chemical Industry Institute of Toxicology, Research Triangle Park, NC 27709.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925598" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Blood Physiological Phenomena ; Blotting, Northern ; Calcium/pharmacology ; Cell Line ; Cloning, Molecular ; Cycloheximide/pharmacology ; Gene Expression Regulation/drug effects ; Humans ; Interleukin-1/*genetics ; *Plasminogen Inactivators ; RNA, Messenger/drug effects ; Tetrachlorodibenzodioxin/*pharmacology ; Transcription, Genetic/drug effects
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  • 60
    Publication Date: 1991-05-17
    Description: The aryl hydrocarbon (Ah) receptor binds various environmental pollutants, such as polycyclic aromatic hydrocarbons, heterocyclic amines, and polychlorinated aromatic compounds (dioxins, dibenzofurans, and biphenyls), and mediates the carcinogenic effects of these agents. The complementary DNA and part of the gene for an 87-kilodalton human protein that is necessary for Ah receptor function have been cloned. The protein is not the ligand-binding subunit of the receptor but is a factor that is required for the ligand-binding subunit to translocate from the cytosol to the nucleus after binding ligand. The requirement for this factor distinguishes the Ah receptor from the glucocorticoid receptor, to which the Ah receptor has been presumed to be similar. Two portions of the 87-kilodalton protein share sequence similarities with two Drosophila proteins, Per and Sim. Another segment of the protein shows conformity to the consensus sequence for the basic helix-loop-helix motif found in proteins that bind DNA as homodimers or heterodimers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoffman, E C -- Reyes, H -- Chu, F F -- Sander, F -- Conley, L H -- Brooks, B A -- Hankinson, O -- CA 16048/CA/NCI NIH HHS/ -- CA 28868/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 May 17;252(5008):954-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, University of California, Los Angeles 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1852076" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Aryl Hydrocarbon Receptor Nuclear Translocator ; Base Sequence ; Cell Line ; Cell Nucleus/metabolism ; Cloning, Molecular ; Cytosol/metabolism ; *DNA-Binding Proteins ; Humans ; Macromolecular Substances ; Molecular Sequence Data ; Molecular Weight ; Oligonucleotide Probes ; Proteins/*genetics/metabolism ; RNA, Messenger/genetics ; Receptors, Aryl Hydrocarbon ; Receptors, Drug/genetics/*metabolism ; Sequence Homology, Nucleic Acid ; Tetrachlorodibenzodioxin/*metabolism ; *Transcription Factors ; Transfection
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  • 61
    Publication Date: 1991-02-01
    Description: Apolipoprotein AI (apoAI) is a lipid-binding protein that participates in the transport of cholesterol and other lipids in the plasma. A complementary DNA clone for a protein that bound to regulatory elements of the apoAI gene was isolated. This protein, designated apoAI regulatory protein-1 (ARP-1), is a novel member of the steroid hormone receptor superfamily. ARP-1 bound to DNA as a dimer, and its dimerization domain was localized to the COOH-terminal region. ARP-1 also bound to a thyroid hormone-responsive element and to regulatory regions of the apoB, apoCIII, insulin, and ovalbumin genes. In cotransfection experiments, ARP-1 downregulated the apoAI gene. The involvement of ARP-1 in the regulation of apoAI gene expression suggests that it may participate in lipid metabolism and cholesterol homeostasis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ladias, J A -- Karathanasis, S K -- New York, N.Y. -- Science. 1991 Feb 1;251(4993):561-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cardiology, Children's Hospital, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1899293" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Apolipoprotein A-I ; Apolipoproteins A/*genetics ; Base Sequence ; COUP Transcription Factor II ; COUP Transcription Factors ; Cloning, Molecular ; DNA/metabolism ; DNA-Binding Proteins/*metabolism ; Gene Expression Regulation ; Humans ; Lipoproteins, HDL/*genetics ; Molecular Sequence Data ; Oligonucleotide Probes ; Receptors, Steroid/*metabolism ; Regulatory Sequences, Nucleic Acid ; *Transcription Factors
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  • 62
    Publication Date: 1991-08-16
    Description: Recombinant cDNA clones that encode two distinct subunits of the transcription factor GA binding protein (GABP) have been isolated. The predicted amino acid sequence of one subunit, GABP alpha, exhibits similarity to the sequence of the product of the ets-1 protooncogene in a region known to encompass the Ets DNA binding domain. The sequence of the second subunit, GABP beta, contains four 33-amino acid repeats located close to the NH2-terminus of the subunit. The sequences of these repeats are similar to repeats in several transmembrane proteins, including Notch from Drosophila melanogaster and Glp-1 and Lin-12 from Caenorhabditis elegans. Avid, sequence-specific binding to DNA required the presence of both polypeptides, revealing a conceptual convergence of nuclear transforming proteins and membrane-anchored proteins implicated in developmentally regulated signal transduction processes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉LaMarco, K -- Thompson, C C -- Byers, B P -- Walton, E M -- McKnight, S L -- New York, N.Y. -- Science. 1991 Aug 16;253(5021):789-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Research Laboratories, Carnegie Institution of Washington, Department of Embryology, Baltimore, MD 21210.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1876836" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Blotting, Northern ; Cloning, Molecular ; DNA-Binding Proteins/*chemistry/genetics ; GA-Binding Protein Transcription Factor ; Gene Expression ; Molecular Sequence Data ; Nuclear Proteins/chemistry/genetics ; Peptides/chemistry ; Proto-Oncogene Protein c-ets-1 ; Proto-Oncogene Proteins/chemistry ; Proto-Oncogene Proteins c-ets ; RNA, Messenger/genetics ; Rats ; Recombinant Proteins ; Transcription Factors/*chemistry/genetics
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  • 63
    Publication Date: 1991-08-02
    Description: Calcium-activated potassium channels mediate many biologically important functions in electrically excitable cells. Despite recent progress in the molecular analysis of voltage-activated K+ channels, Ca(2+)-activated K+ channels have not been similarly characterized. The Drosophila slowpoke (slo) locus, mutations of which specifically abolish a Ca(2+)-activated K+ current in muscles and neurons, provides an opportunity for molecular characterization of these channels. Genomic and complementary DNA clones from the slo locus were isolated and sequenced. The polypeptide predicted by slo is similar to voltage-activated K+ channel polypeptides in discrete domains known to be essential for function. Thus, these results indicate that slo encodes a structural component of Ca(2+)-activated K+ channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Atkinson, N S -- Robertson, G A -- Ganetzky, B -- NS15390/NS/NINDS NIH HHS/ -- T32 GM07131/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Aug 2;253(5019):551-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Genetics, University of Wisconsin, Madison 53706.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1857984" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Calcium/pharmacology ; Chromosome Aberrations ; Chromosome Deletion ; Cloning, Molecular ; DNA/genetics/isolation & purification ; Drosophila/*genetics/physiology ; Exons ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Phenotype ; Potassium Channels/drug effects/*genetics/physiology ; Protein Conformation ; Sequence Homology, Nucleic Acid ; Transcription, Genetic ; Translocation, Genetic
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  • 64
    Publication Date: 1991-05-10
    Description: The Drosophila homeobox segmentation gene fushi tarazu (ftz) is expressed in a seven-stripe pattern during early embryogenesis. This characteristic pattern is largely specified by the zebra element located immediately upstream of the ftz transcriptional start site. The FTZ-F1 protein, one of multiple DNA binding factors that interacts with the zebra element, is implicated in the activation of ftz transcription, especially in stripes 1, 2, 3, and 6. An FTZ-F1 complementary DNA has been cloned by recognition site screening of a Drosophila expression library. The identity of the FTZ-F1 complementary DNA clone was confirmed by immunological cross-reaction with antibodies to FTZ-F1 and by sequence analysis of peptides from purified FTZ-F1 protein. The predicted amino acid sequence of FTZ-F1 revealed that the protein is a member of the nuclear hormone receptor superfamily. This finding raises the possibility that a hormonal ligand affects the expression of a homeobox segmentation gene early in embryonic development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lavorgna, G -- Ueda, H -- Clos, J -- Wu, C -- New York, N.Y. -- Science. 1991 May 10;252(5007):848-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1709303" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Northern ; Blotting, Southern ; Blotting, Western ; Chromosome Mapping ; Cloning, Molecular ; Drosophila Proteins ; Drosophila melanogaster ; Fushi Tarazu Transcription Factors ; Gene Expression Regulation ; Genes, Homeobox ; *Homeodomain Proteins ; Insect Hormones/*chemistry ; Molecular Sequence Data ; Open Reading Frames ; RNA/analysis ; Receptors, Steroid/genetics ; Sequence Homology, Nucleic Acid ; Transcription, Genetic ; Zinc Fingers
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  • 65
    Publication Date: 1991-03-22
    Description: A DNA probe that spanned a domain conserved among the proto-oncogene c-rel, the Drosophila morphogen dorsal, and the p50 DNA binding subunit of NF-kappa B was generated from Jurkat T cell complementary DNA with the polymerase chain reaction (PCR) and degenerate oligonucleotides. This probe was used to identify a rel-related complementary DNA that hybridized to a 2.6-kilobase messenger RNA present in human T and B lymphocytes. In vitro transcription and translation of the complementary DNA resulted in the synthesis of a protein with an apparent molecular size of 65 kilodaltons (kD). The translated protein showed weak DNA binding with a specificity for the kappa B binding motif. This protein-DNA complex comigrated with the complex obtained with the purified human p65 NF-kappa B subunit and binding was inhibited by I kappa B-alpha and -beta proteins. In addition, the 65-kD protein associated with the p50 subunit of NF-kappa B and the kappa B probe to form a complex with the same electrophoretic mobility as the NF-kappa B-DNA complex. Therefore the rel-related 65-kD protein may represent the p65 subunit of the active NF-kappa B transcription factor complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ruben, S M -- Dillon, P J -- Schreck, R -- Henkel, T -- Chen, C H -- Maher, M -- Baeuerle, P A -- Rosen, C A -- New York, N.Y. -- Science. 1991 Mar 22;251(5000):1490-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Oncology and Virology, Roche Institute of Molecular Biology, Roche Research Center, Nutley, NJ 07110-1199.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2006423" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Blotting, Northern ; Cloning, Molecular ; DNA/genetics ; Humans ; Macromolecular Substances ; Molecular Sequence Data ; NF-kappa B/*genetics ; Polymerase Chain Reaction ; Proto-Oncogene Proteins/*genetics ; Proto-Oncogene Proteins c-rel ; T-Lymphocytes
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  • 66
    Publication Date: 1991-11-25
    Description: A calcitonin receptor complementary DNA (cDNA) was cloned by expression of a cDNA library from a porcine kidney epithelial cell line in COS cells. The 482-amino acid receptor has high affinity for salmon calcitonin (dissociation constant Kd approximately 6 nM) and is functionally coupled to increases in intracellular cyclic adenosine monophosphate (cAMP). The receptor shows no sequence similarity to other reported G protein-coupled receptors but is homologous to the parathyroid hormone-parathyroid hormone-related peptide (PTH-PTHrP) receptor, indicating that the receptors for these hormones, which regulate calcium homeostasis, represent a new family of G protein-coupled receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, H Y -- Harris, T L -- Flannery, M S -- Aruffo, A -- Kaji, E H -- Gorn, A -- Kolakowski, L F Jr -- Lodish, H F -- Goldring, S R -- AM 03564/AM/NIADDK NIH HHS/ -- HL-41484/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 15;254(5034):1022-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Cambridge, MA 02142.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1658940" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/physiology ; Amino Acid Sequence ; Animals ; Blotting, Northern ; Calcitonin/*metabolism ; Cloning, Molecular ; Cyclic AMP/physiology ; DNA/genetics ; Gene Expression ; Kidney/physiology ; Molecular Sequence Data ; RNA, Messenger/genetics ; Receptors, Calcitonin ; Receptors, Cell Surface/*genetics ; Swine
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  • 67
    Publication Date: 1991-03-29
    Description: Onchocerciasis (river blindness) is a serious health problem and a severe obstacle to social and economic development, especially in Africa. A complementary DNA fragment coding for an Onchocerca volvulus antigen (OV-16) was cloned and expressed in the plasmid vector pCG808fx. Immune responses to this O. volvulus-specific recombinant antigen were detectable in patients with documented onchocerciasis; the antibody response was also detectable at 3 months and at more than 1 year before infection could otherwise be detected in humans and in chimpanzees experimentally infected with O. volvulus third-stage larvae.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lobos, E -- Weiss, N -- Karam, M -- Taylor, H R -- Ottesen, E A -- Nutman, T B -- New York, N.Y. -- Science. 1991 Mar 29;251(5001):1603-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Parasitic Diseases, National Institutes of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2011741" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Helminth ; Antibody Specificity ; Antigens, Helminth/*analysis/genetics ; Child ; Cloning, Molecular ; Enzyme-Linked Immunosorbent Assay ; Humans ; Mali ; Onchocerca/genetics/*immunology ; Onchocerciasis/*diagnosis/immunology/prevention & control ; Pan troglodytes
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  • 68
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-11-06
    Description: The HM1 gene in maize controls both race-specific resistance to the fungus Cochliobolus carbonum race 1 and expression of the NADPH (reduced form of nicotinamide adenine dinucleotide phosphate)-dependent HC toxin reductase (HCTR), which inactivates HC toxin, a cyclic tetrapeptide produced by the fungus to permit infection. Several HM1 alleles were generated and cloned by transposon-induced mutagenesis. The sequence of wild-type HM1 shares homology with dihydroflavonol-4-reductase genes from maize, petunia, and snap-dragon. Sequence homology is greatest in the beta alpha beta-dinucleotide binding fold that is conserved among NADPH- and NADH (reduced form of nicotinamide adenine dinucleotide)-dependent reductases and dehydrogenases. This indicates that HM1 encodes HCTR.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johal, G S -- Briggs, S P -- New York, N.Y. -- Science. 1992 Nov 6;258(5084):985-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biotechnology Research, Pioneer Hi-Bred International, Inc., Johnston, IA 50131.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1359642" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Blotting, Southern ; Cloning, Molecular ; DNA/chemistry/genetics ; *Genes, Plant ; *Helminthosporium ; Introns ; Molecular Sequence Data ; NADP/pharmacology ; Nucleic Acid Hybridization ; Oxidoreductases/chemistry/*genetics ; Peptides, Cyclic/antagonists & inhibitors ; *Plant Diseases ; *Plant Proteins ; Polymorphism, Restriction Fragment Length ; RNA Splicing ; RNA, Messenger/genetics ; Zea mays/enzymology/*genetics
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  • 69
    Publication Date: 1992-02-21
    Description: The fms-like tyrosine kinase (Flt) is a transmembrane receptor in the tyrosine kinase family. Expression of flt complementary DNA in COS cells conferred specific, high-affinity binding of vascular endothelial growth factor, also known as vascular permeability factor (VEGF-VPF), a factor that induces vascular permeability when injected in the guinea pig skin and stimulates endothelial cell proliferation. Expression of Flt in Xenopus laevis oocytes caused the oocytes to release calcium in response to VEGF-VPF. These findings show that flt encodes a receptor for VEGF-VPF.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de Vries, C -- Escobedo, J A -- Ueno, H -- Houck, K -- Ferrara, N -- Williams, L T -- P01 HL-43821/HL/NHLBI NIH HHS/ -- R01 HL-32898/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1992 Feb 21;255(5047):989-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1312256" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; Cross-Linking Reagents ; Endothelial Growth Factors/*physiology ; Enzyme Activation ; Humans ; In Vitro Techniques ; Lymphokines/*physiology ; Proto-Oncogene Proteins/genetics/*physiology ; Receptors, Cell Surface/*genetics ; Signal Transduction ; Transfection ; Vascular Endothelial Growth Factor A ; Vascular Endothelial Growth Factor Receptor-1 ; Vascular Endothelial Growth Factors ; Xenopus laevis
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  • 70
    Publication Date: 1992-02-21
    Description: The gap genes of Drosophila are the first zygotic genes to respond to the maternal positional signals and establish the body pattern along the anterior-posterior axis. The gap gene knirps, required for patterning in the posterior region of the embryo, can be activated throughout the wild-type embryo and is normally repressed from the anterior and posterior sides. These results provide direct molecular evidence that the posterior morphogen system interacts in a fundamentally different manner than do hunchback and bicoid, which are responsible for anterior pattern formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pankratz, M J -- Busch, M -- Hoch, M -- Seifert, E -- Jackle, H -- New York, N.Y. -- Science. 1992 Feb 21;255(5047):986-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck Institut fur Biophysikalische Chemie, Abteilung Molekulare Entwicklungsbiologie, Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1546296" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Cloning, Molecular ; Drosophila melanogaster/embryology/*genetics ; Gene Expression Regulation ; Genes ; Molecular Sequence Data ; Morphogenesis ; Regulatory Sequences, Nucleic Acid
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  • 71
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-02-28
    Description: The yeast transcription factor IIA (TFIIA), a component of the basal transcription machinery of RNA polymerase II and implicated in vitro in regulation of basal transcription, is composed of two subunits of 32 and 13.5 kilodaltons. The genes that encode these subunits, termed TOA1 and TOA2, respectively, were cloned. Neither gene shares obvious sequence similarity with the other or with any other previously identified genes. The recombinant factor bound to a TATA binding protein-DNA complex and complemented yeast and mammalian in vitro transcription systems depleted of TFIIA. Both the TOA1 and TOA2 genes are essential for growth of yeast.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ranish, J A -- Lane, W S -- Hahn, S -- New York, N.Y. -- Science. 1992 Feb 28;255(5048):1127-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Fred Hutchinson Cancer Research Center, Seattle, WA 98104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1546313" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cloning, Molecular ; DNA Mutational Analysis ; DNA-Binding Proteins/genetics ; *Genes, Fungal ; Molecular Sequence Data ; Recombinant Proteins/metabolism ; Saccharomyces cerevisiae/*genetics ; *Saccharomyces cerevisiae Proteins ; Transcription Factor TFIIA ; Transcription Factors/*genetics ; Transcription, Genetic
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  • 72
    Publication Date: 1992-08-07
    Description: A Src homology 3 (SH3) region is a sequence of approximately 50 amino acids found in many nonreceptor tyrosine kinases and other proteins. Deletion of the SH3 region from the protein encoded by the c-abl proto-oncogene activates the protein's transforming capacity, thereby suggesting the participation of the SH3 region in the negative regulation of transformation. A complementary DNA was isolated that encoded a protein, 3BP-1, to which the SH3 region of Abl bound with high specificity and to which SH3 regions from other proteins bound differentially. The sequence of the 3BP-1 protein is similar to that of a COOH-terminal segment of Bcr and to guanosine triphosphatase-activating protein (GAP)-rho, which suggests that it might have GAP activity for Ras-related proteins. The 3BP-1 protein may therefore be a mediator of SH3 function in transformation inhibition and may link tyrosine kinases to Ras-related proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cicchetti, P -- Mayer, B J -- Thiel, G -- Baltimore, D -- A107233/PHS HHS/ -- CA 08875/CA/NCI NIH HHS/ -- CA51462/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Aug 7;257(5071):803-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1379745" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Amino Acid Sequence ; Animals ; Binding Sites ; Chimera ; Cloning, Molecular ; GTPase-Activating Proteins ; Gene Library ; *Genes, abl ; *Genes, src ; Glutathione Transferase/genetics/metabolism ; Mice ; Molecular Sequence Data ; Oncogene Proteins/genetics/*metabolism ; Plasmids ; Polymerase Chain Reaction/methods ; Prosencephalon/physiology ; Protein-Tyrosine Kinases/*metabolism ; Proteins/*metabolism ; *Proto-Oncogene Proteins ; Proto-Oncogene Proteins c-abl/genetics/*metabolism ; Proto-Oncogene Proteins c-bcr ; Proto-Oncogene Proteins pp60(c-src)/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Restriction Mapping ; Rho Factor/*metabolism ; Sequence Homology, Nucleic Acid ; ras GTPase-Activating Proteins
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  • 73
    Publication Date: 1992-04-03
    Description: Interleukin-1 beta (IL-1 beta) mediates a wide range of immune and inflammatory responses. The active cytokine is generated by proteolytic cleavage of an inactive precursor. A complementary DNA encoding a protease that carries out this cleavage has been cloned. Recombinant expression in COS-7 cells enabled the cells to process precursor IL-1 beta to the mature form. Sequence analysis indicated that the enzyme itself may undergo proteolytic processing. The gene encoding the protease was mapped to chromosomal band 11q23, a site frequently involved in rearrangement in human cancers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cerretti, D P -- Kozlosky, C J -- Mosley, B -- Nelson, N -- Van Ness, K -- Greenstreet, T A -- March, C J -- Kronheim, S R -- Druck, T -- Cannizzaro, L A -- New York, N.Y. -- Science. 1992 Apr 3;256(5053):97-100.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Immunex Corporation, Seattle, WA 98101.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1373520" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Caspase 1 ; Cell Line ; Chromosome Banding ; *Chromosomes, Human, Pair 11 ; Cloning, Molecular ; Enzyme Precursors/biosynthesis/*genetics/isolation & purification ; Humans ; Metalloendopeptidases/biosynthesis/*genetics/isolation & purification ; Molecular Sequence Data ; Neutrophils/enzymology ; Oligodeoxyribonucleotides ; Poly A/genetics/isolation & purification ; Polymerase Chain Reaction/methods ; RNA/genetics/isolation & purification ; RNA, Messenger/genetics ; Recombinant Proteins/biosynthesis/isolation & purification ; Transfection
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  • 74
    Publication Date: 1990-06-08
    Description: X-linked Alport syndrome is a hereditary glomerulonephritis in which progressive loss of kidney function is often accompanied by progressive loss of hearing. Ultrastructural defects in glomerular basement membranes (GBM) of Alport syndrome patients implicate an altered structural protein as the cause of nephritis. The product of COL4A5, the alpha 5(IV) collagen chain, is a specific component of GBM within the kidney, and the gene maps to the same X chromosomal region as does Alport syndrome. Three structural aberrations were found in COL4A5, in intragenic deletion, a Pst I site variant, and an uncharacterized abnormality, which appear to cause nephritis and deafness, with allele-specific severity, in three Alport syndrome kindreds in Utah.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barker, D F -- Hostikka, S L -- Zhou, J -- Chow, L T -- Oliphant, A R -- Gerken, S C -- Gregory, M C -- Skolnick, M H -- Atkin, C L -- Tryggvason, K -- DK 36200/DK/NIDDK NIH HHS/ -- DK 39497/DK/NIDDK NIH HHS/ -- M01 RR 00064/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1990 Jun 8;248(4960):1224-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Informatics, University of Utah School of Medicine, Salt Lake City 84132.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2349482" target="_blank"〉PubMed〈/a〉
    Keywords: Blotting, Southern ; Cloning, Molecular ; Collagen/*genetics ; DNA/genetics/isolation & purification ; Exons ; Female ; *Genes ; Humans ; Male ; Molecular Weight ; *Mutation ; Nephritis, Hereditary/*genetics ; Pedigree ; Restriction Mapping ; X Chromosome
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  • 75
    Publication Date: 1990-04-27
    Description: The beta-amyloid protein (beta/A4), derived from a larger amyloid precursor protein (APP), is the principal component of senile plaques in Alzheimer's disease. APP is an integral membrane glycoprotein and is secreted as a carboxyl-terminal truncated molecule. APP cleavage, which is a membrane-associated event, occurred at a site located within the beta/A4 region. This suggests that an intact amyloidogenic beta/A4 fragment is not generated during normal APP catabolism. Therefore, an early event in amyloid formation may involve altered APP processing that results in the release and subsequent deposition of intact beta/A4.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sisodia, S S -- Koo, E H -- Beyreuther, K -- Unterbeck, A -- Price, D L -- AG 03359/AG/NIA NIH HHS/ -- AG 05146/AG/NIA NIH HHS/ -- AG 07914/AG/NIA NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1990 Apr 27;248(4954):492-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, MD 21205-2181.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1691865" target="_blank"〉PubMed〈/a〉
    Keywords: Aged ; Alzheimer Disease/*metabolism ; Amyloid/genetics/*metabolism ; Amyloid beta-Peptides ; Amyloid beta-Protein Precursor ; Animals ; Cell Membrane ; Cells, Cultured ; Cloning, Molecular ; DNA, Recombinant ; Glycosylation ; Half-Life ; Humans ; Immunoblotting ; Molecular Weight ; Plasmids ; Protein Precursors/genetics/*metabolism ; *Protein Processing, Post-Translational ; Recombinant Fusion Proteins/metabolism ; Substance P/genetics ; Transfection
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  • 76
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-12-14
    Description: Introns have been found in the genomes of all major groups of organisms except eubacteria. The presence of introns in chloroplasts and mitochondria, both of which are of eubacterial origin, has been interpreted as evidence either for the recent acquisition of introns by organelles or for the loss of introns from their eubacterial progenitors. The gene for the leucine transfer RNA with a UAA anticodon [tRNALeu (UAA)] from five diverse cyanobacteria and several major groups of chloroplasts contains a single group I intron. The intron is conserved in secondary structure and primary sequence, and occupies the same position, within the UAA anticodon. The homology of the intron across chloroplasts and cyanobacteria implies that it was present in their common ancestor and that it has been maintained in their genomes for at least 1 billion years.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuhsel, M G -- Strickland, R -- Palmer, J D -- 35087/PHS HHS/ -- New York, N.Y. -- Science. 1990 Dec 14;250(4987):1570-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Indiana University, Bloomington 47405.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2125748" target="_blank"〉PubMed〈/a〉
    Keywords: Anticodon/genetics ; Base Sequence ; Biological Evolution ; Chloroplasts/*metabolism ; Cloning, Molecular ; Cyanobacteria/genetics ; Eubacterium/*genetics ; Eukaryota/genetics ; Introns/*genetics ; Molecular Sequence Data ; Nucleic Acid Conformation ; Plants/genetics ; Polymerase Chain Reaction ; RNA, Transfer, Leu/*genetics
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  • 77
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-10-05
    Description: In its wild-type form, the protein p53 can interfere with neoplastic processes. Tumor-derived cells often express mutant p53. Full-length mutant forms of p53 isolated so far from transformed mouse cells exhibit three common properties in vitro: loss of transformation-suppressing activity, gain of pronounced transforming potential, and ability to bind the heat shock protein cognate hsc70. A tumor-derived mouse p53 variant is now described, whose site of mutation corresponds to a hot spot for p53 in human tumors. While absolutely nonsuppressing, it is only weakly transforming and exhibits no detectable hsc70 binding. The data suggest that the ability of a p53 mutant to bind endogenous p53 is not the sole determinant of its oncogenic potential. The data also support the existence of gain-of-function p53 mutants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Halevy, O -- Michalovitz, D -- Oren, M -- R01 CA40099/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1990 Oct 5;250(4977):113-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical Immunology, Weizmann Institute of Science, Rehovot, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2218501" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cell Transformation, Neoplastic ; Cloning, Molecular ; Humans ; Mice ; *Mutation ; Nuclear Proteins/*genetics ; Plasmids ; Polymerase Chain Reaction ; RNA, Messenger/genetics ; Rats ; Transfection ; Tumor Suppressor Protein p53/*genetics/physiology
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  • 78
    Publication Date: 1990-01-05
    Description: Allelic deletions involving chromosome 18q occur in more than 70 percent of colorectal cancers. Such deletions are thought to signal the existence of a tumor suppressor gene in the affected region, but until now a candidate suppressor gene on this chromosomal arm had not been identified. A contiguous stretch of DNA comprising 370 kilobase pairs (kb) has now been cloned from a region of chromosome 18q suspected to reside near this gene. Potential exons in the 370-kb region were defined by human-rodent sequence identities, and the expression of potential exons was assessed by an "exon-connection" strategy based on the polymerase chain reaction. Expressed exons were used as probes for cDNA screening to obtain clones that encoded a portion of a gene termed DCC; this cDNA was encoded by at least eight exons within the 370-kb genomic region. The predicted amino acid sequence of the cDNA specified a protein with sequence similarity to neural cell adhesion molecules and other related cell surface glycoproteins. While the DCC gene was expressed in most normal tissues, including colonic mucosa, its expression was greatly reduced or absent in most colorectal carcinomas tested. Somatic mutations within the DCC gene observed in colorectal cancers included a homozygous deletion of the 5' end of the gene, a point mutation within one of the introns, and ten examples of DNA insertions within a 0.17-kb fragment immediately downstream of one of the exons. The DCC gene may play a role in the pathogenesis of human colorectal neoplasia, perhaps through alteration of the normal cell-cell interactions controlling growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fearon, E R -- Cho, K R -- Nigro, J M -- Kern, S E -- Simons, J W -- Ruppert, J M -- Hamilton, S R -- Preisinger, A C -- Thomas, G -- Kinzler, K W -- CA 09243/CA/NCI NIH HHS/ -- GM07184/GM/NIGMS NIH HHS/ -- GM07309/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1990 Jan 5;247(4938):49-56.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Oncology Center, Johns Hopkins University School of Medicine, Baltimore, MD 21231.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2294591" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Northern ; Blotting, Southern ; Cell Adhesion Molecules, Neuronal/genetics ; *Chromosome Deletion ; *Chromosomes, Human, Pair 18 ; Cloning, Molecular ; Colorectal Neoplasms/*genetics ; Cross Reactions ; DNA Probes ; DNA, Neoplasm/*genetics ; Exons ; Gene Expression Regulation, Neoplastic ; Humans ; Molecular Sequence Data ; Polymerase Chain Reaction ; RNA, Neoplasm/genetics ; Sequence Homology, Nucleic Acid ; *Suppression, Genetic ; Tumor Cells, Cultured
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  • 79
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-02-23
    Description: Substance P is a member of the tachykinin peptide family and participates in the regulation of diverse biological processes. The polymerase chain reaction and conventional library screening were used to isolate a complementary DNA (cDNA) encoding the rat substance P receptor from brain and submandibular gland. By homology analysis, this receptor belongs to the G protein-coupled receptor superfamily. The receptor cDNA was expressed in a mammalian cell line and the ligand binding properties of the encoded receptor were pharmacologically defined by Scatchard analysis and tachykinin peptide displacement as those of a substance P receptor. The distribution of the messenger RNA for this receptor is highest in urinary bladder, submandibular gland, striatum, and spinal cord, which is consistent with the known distribution of substance P receptor binding sites. Thus, this receptor appears to mediate the primary actions of substance P in various brain regions and peripheral tissues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hershey, A D -- Krause, J E -- NS21937/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1990 Feb 23;247(4945):958-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy and Neurobiology, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2154852" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Brain Chemistry ; Cloning, Molecular ; DNA/*genetics/isolation & purification ; GTP-Binding Proteins/metabolism ; Gene Expression ; Intestine, Small/analysis ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Polymerase Chain Reaction ; RNA, Messenger/analysis ; Rats ; Receptors, Neurokinin-1 ; Receptors, Neurotransmitter/*genetics ; Sequence Homology, Nucleic Acid ; Submandibular Gland/analysis ; Tissue Distribution ; Urinary Bladder/analysis
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  • 80
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-06-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, L -- New York, N.Y. -- Science. 1990 Jun 15;248(4961):1310-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2356467" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Base Sequence ; Caenorhabditis/*genetics/growth & development ; *Chromosome Mapping ; Cloning, Molecular ; DNA/genetics ; Genomic Library ; Human Genome Project ; Nucleotide Mapping
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  • 81
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-12-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1990 Dec 21;250(4988):1749.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2125369" target="_blank"〉PubMed〈/a〉
    Keywords: Blotting, Southern ; Chromosomes, Human, Pair 17 ; Chromosomes, Human, Pair 22 ; Cloning, Molecular ; DNA/genetics ; Humans ; Neurofibromatosis 1/*genetics ; Translocation, Genetic
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  • 82
    Publication Date: 1990-11-09
    Description: Expression of the human T cell receptor (TCR) alpha gene is regulated by a T cell-specific transcriptional enhancer that is located 4.5 kilobases (kb) 3' to the C alpha gene segment. The core enhancer contains two nuclear protein binding sites, T alpha 1 and T alpha 2, which are essential for full enhancer activity. T alpha 1 contains a consensus cyclic adenosine monophosphate (cAMP) response element (CRE) and binds a set of ubiquitously expressed CRE binding proteins. In contrast, the transcription factors that interact with the T alpha 2 site have not been defined. In this report, a lambda gt11 expression protocol was used to isolate a complementary DNA (cDNA) that programs the expression of a T alpha 2 binding protein. DNA sequence analysis demonstrated that this clone encodes the human ets-1 proto-oncogene. Lysogen extracts produced with this cDNA clone contained a beta-galactosidase-Ets-1 fusion protein that bound specifically to a synthetic T alpha 2 oligonucleotide. The Ets-1 binding site was localized to a 17-base pair (bp) region from the 3' end of T alpha 2. Mutation of five nucleotides within this sequence abolished both Ets-1 binding and the activity of the TCR alpha enhancer in T cells. These results demonstrate that Ets-1 binds in a sequence-specific fashion to the human TCR alpha enhancer and suggest that this developmentally regulated proto-oncogene functions in regulating TCR alpha gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ho, I C -- Bhat, N K -- Gottschalk, L R -- Lindsten, T -- Thompson, C B -- Papas, T S -- Leiden, J M -- AI-29673/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1990 Nov 9;250(4982):814-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Ann Arbor, MI.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2237431" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding, Competitive ; Cloning, Molecular ; DNA/genetics ; DNA Mutational Analysis ; *Enhancer Elements, Genetic ; Gene Expression Regulation ; Gene Rearrangement, T-Lymphocyte ; Humans ; Immunoblotting ; Molecular Sequence Data ; Proto-Oncogene Protein c-ets-1 ; Proto-Oncogene Proteins/genetics/*metabolism ; Proto-Oncogene Proteins c-ets ; *Proto-Oncogenes ; Receptors, Antigen, T-Cell/genetics/*metabolism ; Transcription Factors ; Transcription, Genetic
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  • 83
    Publication Date: 1990-12-21
    Description: A heparin binding mitogenic protein isolated from bovine uterus shares NH2-terminal amino acid sequence with a protein isolated from newborn rat brain. The cDNA's of the bovine, human, and rat genes have been isolated and encode extraordinarily conserved proteins unrelated to known growth or neurotrophic factors, although identity of nearly 50 percent has been found with the predicted sequence of a retinoic acid induced transcript in differentiating mouse embryonal carcinoma cells. Lysates of COS-7 cells transiently expressing this protein were mitogenic for NRK cells and initiated neurite outgrowth from mixed cultures of embryonic rat brain cells. RNA transcripts encoding this protein were widely distributed in tissues and were developmentally regulated. This protein, previously designated as heparin binding growth factor (HBGF)-8, is now renamed pleiotrophin (PTN) to reflect its diverse activities. PTN may be the first member of a family of developmentally regulated cytokines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Y S -- Milner, P G -- Chauhan, A K -- Watson, M A -- Hoffman, R M -- Kodner, C M -- Milbrandt, J -- Deuel, T F -- CA49712/CA/NCI NIH HHS/ -- HL14147/HL/NHLBI NIH HHS/ -- HL31102/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1990 Dec 21;250(4988):1690-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Jewish Hospital, Washington University Medical Center, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2270483" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Axons/*physiology/ultrastructure ; Base Sequence ; Brain/*metabolism ; *Carrier Proteins ; Cattle ; Cell Division ; Cell Line ; Cloning, Molecular ; Cytokines/*genetics ; Humans ; Mitogens/*genetics ; Molecular Sequence Data ; Organ Specificity ; Rats ; Sequence Homology, Nucleic Acid ; Transfection
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  • 84
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-12-14
    Description: Mutations of the gene encoding p53, a 53-kilodalton cellular protein, are found frequently in human tumor cells, suggesting a crucial role for this gene in human oncogenesis. To model the stepwise mutation or loss of both p53 alleles during tumorigenesis, a human osteosarcoma cell line, Saos-2, was used that completely lacked endogenous p53. Single copies of exogenous p53 genes were then introduced by infecting cells with recombinant retroviruses containing either point-mutated or wild-type versions of the p53 cDNA sequence. Expression of wild-type p53 suppressed the neoplastic phenotype of Saos-2 cells, whereas expression of mutated p53 conferred a limited growth advantage to cells in the absence of wild-type p53. Wild-type p53 was phenotypically dominant to mutated p53 in a two-allele configuration. These results suggest that, as with the retinoblastoma gene, mutation of both alleles of the p53 gene is essential for its role in oncogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, P L -- Chen, Y M -- Bookstein, R -- Lee, W H -- CA51495/CA/NCI NIH HHS/ -- EY00278/EY/NEI NIH HHS/ -- EY05758/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1990 Dec 14;250(4987):1576-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, School of Medicine, University of California, San Diego, La Jolla 92093-0612.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2274789" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Base Sequence ; *Cinnamates ; Cloning, Molecular ; DNA/genetics ; Drug Resistance/genetics ; Genes, p53/*genetics ; Genetic Vectors ; Humans ; Hygromycin B/analogs & derivatives ; Molecular Sequence Data ; Moloney murine leukemia virus/genetics ; Mutation ; Neomycin ; Osteosarcoma/*genetics ; Plasmids ; Transfection ; Tumor Cells, Cultured
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  • 85
    Publication Date: 1990-06-29
    Description: Transcription factor IID (TFIID) binds to the TATA box promoter element and regulates the expression of most eukaryotic genes transcribed by RNA polymerase II. Complementary DNA (cDNA) encoding a human TFIID protein has been cloned. The human TFIID polypeptide has 339 amino acids and a molecular size of 37,745 daltons. The carboxyl-terminal 181 amino acids of the human TFIID protein shares 80% identity with the TFIID protein from Saccharomyces cerevisiae. The amino terminus contains an unusual repeat of 38 consecutive glutamine residues and an X-Thr-Pro repeat. Expression of DNA in reticulocyte lysates or in Escherichia coli yielded a protein that was competent for both DNA binding and transcription activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kao, C C -- Lieberman, P M -- Schmidt, M C -- Zhou, Q -- Pei, R -- Berk, A J -- CA25235/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1990 Jun 29;248(4963):1646-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Molecular Biology Institute, University of California, Los Angeles 90024-1570.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2194289" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cloning, Molecular ; Escherichia coli/genetics ; Gene Expression ; HeLa Cells/metabolism ; Humans ; Molecular Sequence Data ; *Promoter Regions, Genetic ; Recombinant Proteins/metabolism ; Reticulocytes/metabolism ; Saccharomyces cerevisiae/*genetics ; Sequence Homology, Nucleic Acid ; Transcription Factor TFIID ; Transcription Factors/*genetics/metabolism ; *Transcription, Genetic
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  • 86
    Publication Date: 1990-03-16
    Description: Prothoracicotropic hormone (PTTH), a brain secretory polypeptide of insects, stimulates the prothoracic glands to produce and release ecdysone, the steroid essential to insect development. The complementary DNAs encoding PTTH of the silkmoth Bombyx mori were cloned and characterized, and the complete amino acid sequence was deduced. The data indicated that PTTH is first synthesized as a 224-amino acid polypeptide precursor containing three proteolytic cleavage signals. The carboxyl-terminal component (109 amino acids) that follows the last cleavage signal represents one PTTH subunit. Two PTTH subunits are linked together by disulfide bonds, before or after cleavage from prepro-PTTH, to form a homodimeric PTTH. When introduced into Escherichia coli cells, the complementary DNA directed the expression of an active substance that was functionally indistinguishable from natural PTTH. In situ hybridization showed the localization of the prepro-PTTH mRNA to two dorsolateral neurosecretory cells of the Bombyx brain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kawakami, A -- Kataoka, H -- Oka, T -- Mizoguchi, A -- Kimura-Kawakami, M -- Adachi, T -- Iwami, M -- Nagasawa, H -- Suzuki, A -- Ishizaki, H -- New York, N.Y. -- Science. 1990 Mar 16;247(4948):1333-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, School of Science, Nagoya University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2315701" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Bombyx/*genetics/physiology ; Cloning, Molecular ; DNA/genetics ; Gene Expression ; Insect Hormones/*genetics ; Molecular Sequence Data ; Neurosecretory Systems/physiology ; Nucleic Acid Hybridization ; Protein Precursors/genetics
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  • 87
    Publication Date: 1990-03-09
    Description: Certain RNA molecules, called ribozymes, possess enzymatic, self-cleaving activity. The cleavage reaction is catalytic and no energy source is required. Ribozymes of the "hammerhead" motif were identified in plant RNA pathogens. These ribozymes possess unique secondary (and possibly tertiary) structures critical for their cleavage ability. The present study shows precise cleavage of human immunodeficiency virus type 1 (HIV-1) sequences in a cell-free system by hammerhead ribozymes. In addition to the cell-free studies, human cells stably expressing a hammerhead ribozyme targeted to HIV-1 gag transcripts have been constructed. When these cells were challenged with HIV-1, a substantial reduction in the level of HIV-1 gag RNA relative to that in nonribozyme-expressing cells, was observed. The reduction in gag RNA was reflected in a reduction in antigen p24 levels. These results suggest the feasibility of developing ribozymes as therapeutic agents against human pathogens such as HIV-1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sarver, N -- Cantin, E M -- Chang, P S -- Zaia, J A -- Ladne, P A -- Stephens, D A -- Rossi, J J -- AI25959/AI/NIAID NIH HHS/ -- CA34991/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1990 Mar 9;247(4947):1222-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Research and Development Program, National Institute of Allergy and Infectious Diseases, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2107573" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*drug therapy ; Base Sequence ; Catalysis ; Cloning, Molecular ; Gene Expression ; Gene Products, gag/metabolism ; Genes, gag/*drug effects ; HIV Core Protein p24 ; HIV-1/*drug effects/genetics ; HeLa Cells ; Humans ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Polymerase Chain Reaction ; RNA, Catalytic ; RNA, Ribosomal/*pharmacology/therapeutic use ; RNA, Viral/*drug effects ; Transfection ; Viral Core Proteins/metabolism
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  • 88
    Publication Date: 1991-03-08
    Description: The myc protooncogene family has been implicated in cell proliferation, differentiation, and neoplasia, but its mechanism of function at the molecular level is unknown. The carboxyl terminus of Myc family proteins contains a basic region helix-loop-helix leucine zipper motif (bHLH-Zip), which has DNA-binding activity and has been predicted to mediate protein-protein interactions. The bHLH-Zip region of c-Myc was used to screen a complementary DNA (cDNA) expression library, and a bHLH-Zip protein, termed Max, was identified. Max specifically associated with c-Myc, N-Myc, and L-Myc proteins, but not with a number of other bHLH, bZip, or bHLH-Zip proteins. The interaction between Max and c-Myc was dependent on the integrity of the c-Myc HLH-Zip domain, but not on the basic region or other sequences outside the domain. Furthermore, the Myc-Max complex bound to DNA in a sequence-specific manner under conditions where neither Max nor Myc exhibited appreciable binding. The DNA-binding activity of the complex was dependent on both the dimerization domain and the basic region of c-Myc. These results suggest that Myc family proteins undergo a restricted set of interactions in the cell and may belong to the more general class of eukaryotic DNA-binding transcription factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Blackwood, E M -- Eisenman, R N -- P01 CA28151/CA/NCI NIH HHS/ -- R01 CA20525/CA/NCI NIH HHS/ -- T32 CA09437/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Mar 8;251(4998):1211-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, WA 98104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2006410" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors ; Basic-Leucine Zipper Transcription Factors ; Cloning, Molecular ; DNA-Binding Proteins/*genetics/metabolism ; Escherichia coli/genetics ; Gene Library ; *Genes, myc ; Glutathione Transferase/genetics/metabolism ; Humans ; Molecular Sequence Data ; Oligonucleotide Probes ; Protein Biosynthesis ; Proto-Oncogene Proteins c-myc/*genetics/metabolism ; Recombinant Fusion Proteins/metabolism ; Sequence Homology, Nucleic Acid ; *Transcription Factors ; Transcription, Genetic
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  • 89
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-09-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cherfas, J -- New York, N.Y. -- Science. 1991 Sep 20;253(5026):1354-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1910205" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; DNA/*genetics ; Egypt ; Florida ; *Fossils ; Haplorhini/*genetics ; Humans ; *Mummies ; Plants/genetics
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  • 90
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-10-04
    Description: The CD19-CR2 complex of B lymphocytes contains proteins that participate in two host-defense systems, the immune and complement systems. The ligand for the subunit of the immune system, CD19, is not known, but the complement receptor subunit, CR2 (CD21), binds activation fragments of the C3 component of the complement system and may mediate immunopotentiating effects of complement. A recombinant, soluble CR2 was prepared by fusing the C3-binding region of the receptor to immunoglobulin G1 (IgG1). The (CR2)2-IgG1 chimera competed with cellular CR2 for C3 binding and suppressed the antibody response to a T cell-dependent antigen when administered to mice at the time of immunization. This inhibitory effect of (CR2)2-IgG1 demonstrates the B cell-activating function of the CD19-CR2 complex and suggests a new method for humoral immunosuppression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hebell, T -- Ahearn, J M -- Fearon, D T -- AI-22833/AI/NIAID NIH HHS/ -- AI-28191/AI/NIAID NIH HHS/ -- GM-43803/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 4;254(5028):102-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1718035" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Antibody Formation ; Antigens, CD/*physiology ; Antigens, CD19 ; Antigens, Differentiation, B-Lymphocyte/chemistry/*physiology ; B-Lymphocytes/*physiology ; Base Sequence ; Binding, Competitive ; Cloning, Molecular ; Immunosuppression ; In Vitro Techniques ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C3H ; Molecular Sequence Data ; Receptors, Complement/chemistry/*physiology ; Receptors, Complement 3d ; Recombinant Fusion Proteins ; Signal Transduction ; Solubility
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  • 91
    Publication Date: 1991-03-08
    Description: Yeast artificial chromosomes (YACs) were obtained from a 550-kilobase region that contains three probes previously mapped as very close to the locus of the fragile X syndrome. These YACs spanned the fragile site in Xq27.3 as shown by fluorescent in situ hybridization. An internal 200-kilobase segment contained four chromosomal breakpoints generated by induction of fragile X expression. A single CpG island was identified in the cloned region between markers DXS463 and DXS465 that appears methylated in mentally retarded fragile X males, but not in nonexpressing male carriers of the mutation nor in normal males. This CpG island may indicate the presence of a gene involved in the clinical phenotype of the syndrome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heitz, D -- Rousseau, F -- Devys, D -- Saccone, S -- Abderrahim, H -- Le Paslier, D -- Cohen, D -- Vincent, A -- Toniolo, D -- Della Valle, G -- New York, N.Y. -- Science. 1991 Mar 8;251(4998):1236-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de Genetique Moleculaire des Eucaryotes du CNRS, Institut de Chimie Biologique, Faculte de Medecine, Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2006411" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromosomes, Fungal ; Cloning, Molecular ; DNA Probes ; *Dinucleoside Phosphates ; Fragile X Syndrome/*genetics ; Humans ; Male ; Molecular Sequence Data ; Mutation ; Nucleic Acid Hybridization ; Oligonucleotide Probes ; Polymerase Chain Reaction ; Reference Values ; Restriction Mapping ; Saccharomyces cerevisiae/genetics ; *X Chromosome
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  • 92
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-12-06
    Description: Heterotrimeric guanine nucleotide-binding regulatory proteins (G proteins) dissociate into guanosine triphosphate (GTP)-bound alpha subunits and a complex of beta and gamma subunits after interaction with receptors. The GTP-alpha subunit complex activates appropriate effectors, such as adenylyl cyclase, retinal phosphodiesterase, phospholipase C, and ion channels. G protein beta gamma subunits have been found to have regulatory effects on certain types of adenylyl cyclase. In the presence of Gs alpha, the alpha subunit of the G protein that activates adenylyl cyclase, one form of adenylyl cyclase was inhibited by beta gamma, some forms were activated by beta gamma, and some forms were not affected by beta gamma. These interactions suggest mechanisms for communication between distinct signal-transducing pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tang, W J -- Gilman, A G -- GM34497/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Dec 6;254(5037):1500-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pharmacology, University of Texas Southwestern Medical Center, Dallas 75235.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1962211" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/classification/genetics/*metabolism ; Animals ; Base Sequence ; Cattle ; Cloning, Molecular ; Enzyme Activation ; GTP-Binding Proteins/*physiology ; Guanosine Triphosphate/physiology ; Molecular Sequence Data ; Oligodeoxyribonucleotides/chemistry ; Rabbits ; Recombinant Proteins
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  • 93
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-10-25
    Description: A complementary DNA clone for a serotonin (5HT) transporter has been isolated from rat basophilic leukemia cells. The complementary DNA sequence predicts a 653-amino acid protein with 12 to 13 putative transmembrane domains. The 5HT transporter has significant homology to the gamma-aminobutyric acid, dopamine, and norepinephrine transporters. Uptake by CV-1 cells expressing the transporter complementary DNA resembles 5HT uptake by platelets and brain synaptosomes; it is sensitive to antidepressants, amphetamine derivatives, and cocaine.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoffman, B J -- Mezey, E -- Brownstein, M J -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):579-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cell Biology, National Institute of Mental Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948036" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antidepressive Agents/*pharmacology ; Base Sequence ; Carrier Proteins/drug effects/*genetics/metabolism ; Cell Line ; Cloning, Molecular ; Kinetics ; Leukemia, Basophilic, Acute ; Molecular Sequence Data ; Oligonucleotide Probes ; Rats ; Serotonin/*metabolism ; Transfection
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  • 94
    Publication Date: 1991-10-04
    Description: LIV-I, a high-affinity system that transports neutral, branched-chain amino acids into Escherichia coli, has two components, LivG and LivF, that are homologous to the cystic fibrosis (CF) transmembrane conductance regulator (CFTR). CF-associated mutations of human CFTR were introduced into corresponding regions of LivG, and their effects on leucine transport could be grouped into three classes. Mutations were found that (i) abolished LIV-I--directed transport, (ii) retained about a quarter of wild-type activity at the Michaelis-Menten constant (KM), and (iii) had minimal activity at the KM. A mutation equivalent to a benign polymorphism had no effect on transport. The correlation of these mutational phenotypes in LivG and CFTR suggests that the LIV-I prokaryotic transporter is functionally similar to the CF protein and that this similarity can be exploited to clarify the properties of the nucleotide-binding fold in this superfamily of proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibson, A L -- Wagner, L M -- Collins, F S -- Oxender, D L -- New York, N.Y. -- Science. 1991 Oct 4;254(5028):109-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, University of Michigan, Ann Arbor 48109.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1718037" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters ; Amino Acid Sequence ; Bacterial Proteins/*genetics ; Biological Transport, Active ; Cloning, Molecular ; Cystic Fibrosis/*genetics ; Cystic Fibrosis Transmembrane Conductance Regulator ; DNA Mutational Analysis ; Escherichia coli/genetics ; *Escherichia coli Proteins ; Humans ; Kinetics ; Leucine/metabolism ; Membrane Proteins/*genetics ; *Membrane Transport Proteins ; Molecular Sequence Data ; Protein Binding ; Restriction Mapping ; Sequence Alignment ; Structure-Activity Relationship
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 95
    Publication Date: 1991-09-13
    Description: Interleukin-8 (IL-8) is a member of a family of pro-inflammatory cytokines. Although the best characterized activities of IL-8 include the chemoattraction and activation of neutrophils, other members of this family have a wide range of specific actions including the chemotaxis and activation of monocytes, the selective chemotaxis of memory T cells, the inhibition of hematopoietic stem cell proliferation, and the induction of neutrophil infiltration in vivo. A complementary DNA encoding the IL-8 receptor from human neutrophils has now been isolated. The amino acid sequence shows that the receptor is a member of the superfamily of receptors that couple to guanine nucleotide binding proteins (G proteins). The sequence is 29% identical to that of receptors for the other neutrophil chemoattractants, fMet-Leu-Phe and C5a. Mammalian cells transfected with the IL-8 receptor cDNA clone bind IL-8 with high affinity and respond specifically to IL-8 by transiently mobilizing calcium. The IL-8 receptor may be part of a subfamily of related G protein-coupled receptors that transduce signals for the IL-8 family of pro-inflammatory cytokines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holmes, W E -- Lee, J -- Kuang, W J -- Rice, G C -- Wood, W I -- New York, N.Y. -- Science. 1991 Sep 13;253(5025):1278-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Genentech, Inc., South San Francisco, CA 94080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1840701" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Cloning, Molecular ; DNA Probes ; Humans ; Interleukin-8/*metabolism ; Kinetics ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Plasmids ; RNA, Messenger/genetics ; Receptors, Immunologic/*genetics/metabolism ; Receptors, Interleukin-8A ; Recombinant Proteins/metabolism ; Sequence Homology, Nucleic Acid ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 96
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-01-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, L -- New York, N.Y. -- Science. 1991 Jan 18;251(4991):260-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1898994" target="_blank"〉PubMed〈/a〉
    Keywords: Cloning, Molecular ; Cystic Fibrosis/genetics ; Humans ; Molecular Biology/*standards ; Neurofibromatosis 1/genetics ; Publishing/*standards ; Time Factors
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 97
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-10-04
    Description: Voltage-gated sodium channels, which are responsible for the generation of action potentials in the brain, are phosphorylated by protein kinase C (PKC) in purified form. Activation of PKC decreases peak sodium current up to 80 percent and slows its inactivation for sodium channels in rat brain neurons and for rat brain type IIA sodium channel alpha subunits heterologously expressed in Chinese hamster ovary cells. These effects are specific for PKC because they can be blocked by specific peptide inhibitors of PKC and can be reproduced by direct application of PKC to the cytoplasmic surface of sodium channels in excised inside-out membrane patches. Modulation of brain sodium channels by PKC is likely to have important effects on signal transduction and synaptic transmission in the central nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Numann, R -- Catterall, W A -- Scheuer, T -- NS15751/NS/NINDS NIH HHS/ -- NS25704/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 4;254(5028):115-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1656525" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/physiology ; CHO Cells ; Cloning, Molecular ; Cricetinae ; Diglycerides/pharmacology ; In Vitro Techniques ; Neurons/physiology ; Phosphoproteins/physiology ; Phosphorylation ; Protein Kinase C/*physiology ; Protein Kinases/physiology ; Rats ; Sodium/*physiology ; Sodium Channels/*physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 98
    Publication Date: 1991-09-23
    Description: The Rel-associated protein pp40 is functionally related to I kappa B, an inhibitor of the transcription factor NF-kappa B. Purified pp40 inhibits the DNA binding activity of the NF-kappa B protein complex (p50:p65 heterodimers), p50:c-Rel heteromers, and c-Rel homodimers. The sequence of the complementary DNA encoding pp40 revealed similarity to the gene encoding MAD-3, a protein with mammalian I kappa B-like activity. Protein sequencing of I kappa B purified from rabbit lung confirmed that MAD-3 encodes a protein similar to I kappa B. The sequence similarity between MAD-3 and pp40 includes a casein kinase II and consensus tyrosine phosphorylation site, as well as five repeats of a sequence found in the human erythrocyte protein ankyrin. These results suggest that rel-related transcription factors, which are capable of cytosolic to nuclear translocation, may be held in the cytosol by interaction with related cytoplasmic anchor molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, N -- Ghosh, S -- Simmons, D L -- Tempst, P -- Liou, H C -- Baltimore, D -- Bose, H R Jr -- CA09583/CA/NCI NIH HHS/ -- CA2616/CA/NCI NIH HHS/ -- CA33192/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Sep 13;253(5025):1268-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of Texas, Austin 78712.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1891714" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cells, Cultured ; Chick Embryo ; Cloning, Molecular ; DNA Probes ; Molecular Sequence Data ; NF-kappa B/*antagonists & inhibitors ; Oligonucleotide Probes ; Oncogene Proteins v-rel ; Open Reading Frames ; Phosphoproteins/*genetics/metabolism ; Protein-Tyrosine Kinases/antagonists & inhibitors ; RNA, Messenger/genetics ; Retroviridae Proteins, Oncogenic/*antagonists & inhibitors ; Sequence Homology, Nucleic Acid ; Transcription Factors/*antagonists & inhibitors
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 99
    Publication Date: 1992-05-04
    Description: The molecular basis of skeletal muscle lineage determination was investigated by analyzing DNA control elements that regulate the myogenic determination gene myoD. A distal enhancer was identified that positively regulates expression of the human myoD gene. The myoD enhancer and promoter were active in myogenic and several nonmyogenic cell lines. In transgenic mouse embryos, however, the myoD enhancer and promoter together directed expression of a lacZ transgene specifically to the skeletal muscle lineage. These data suggest that during development myoD is regulated by mechanisms that restrict accessibility of myoD control elements to positive trans-acting factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldhamer, D J -- Faerman, A -- Shani, M -- Emerson, C P Jr -- CA-06927/CA/NCI NIH HHS/ -- HD-07796/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 24;256(5056):538-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Cancer Research, Fox Chase Cancer Center, Philadelphia, PA 19111.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1315077" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cell Line ; Chloramphenicol O-Acetyltransferase/genetics ; Cloning, Molecular ; Enhancer Elements, Genetic ; *Gene Expression Regulation ; Humans ; Mice ; Mice, Transgenic ; Muscle Proteins/*genetics ; Muscles/embryology/metabolism ; MyoD Protein ; Promoter Regions, Genetic ; Transcription, Genetic ; Transfection ; Tumor Cells, Cultured ; beta-Galactosidase/genetics
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 100
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-08-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wallace, B M -- Lasker, J S -- New York, N.Y. -- Science. 1992 Aug 28;257(5074):1211-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1519057" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; DNA/radiation effects ; DNA Damage ; Gene Expression/*radiation effects ; Genes, Viral/*radiation effects ; HIV/*genetics ; HIV Long Terminal Repeat ; Humans ; Mice ; PUVA Therapy/adverse effects ; Sunlight/adverse effects ; Ultraviolet Rays/*adverse effects
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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